CRISPRimmunity

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Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Self targeting spacer number	Target MGE spacer number	Prophage number	Anti-CRISPR protein number
NZ_CP029149	Bergeyella cardium strain HPQL chromosome, complete genome	13 crisprs	DEDDh,cas9,cas1,cas2,cas3,RT	2	17	1	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP029149_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP029149_1

276078-276191

Orphan

Consensus_repeat	Method
TTTTTCTTTAGAAATGAAAAAATATGAATATTAAATATA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP029149_1

>merge|NZ_CP029149|1|276078-276191|CRISPRCasFinder
TTTTTCTTTAGAAATGAAAAAATATGAATATTAAATATAAAACAAAGGCTATCTTGAAAGATAGCCTTTATAATATTTTTCTTTAGAAATGAAAAAATATGAATATTAAATATA

>NZ_CP029149|1|1|276078-276191|CRISPRCasFinder
TTTTTCTTTAGAAATGAAAAAATATGAATATTAAATATA	AAACAAAGGCTATCTTGAAAGATAGCCTTTATAATA
TTTTTCTTTAGAAATGAAAAAATATGAATATTAAATATA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP029149.1\|WP_160223731.1\|264862_265339_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_160223743.1\|278560_280765_+\|peptidase-domain-containing-ABC-transporter	unknown	unknown	gnl\|CDD\|225183
NZ_CP029149.1\|WP_160223736.1\|271939_272218_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_160223744.1\|280754_282059_+\|HlyD-family-efflux-transporter-periplasmic-adaptor-subunit	unknown	unknown	gnl\|CDD\|130902
NZ_CP029149.1\|WP_160223745.1\|282062_283397_+\|TolC-family-protein	unknown	unknown	gnl\|CDD\|224455
NZ_CP029149.1\|WP_160223732.1\|265382_265634_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_160223738.1\|272835_274290_-\|relaxase/mobilization-nuclease-domain-containing-protein	unknown	unknown	gnl\|CDD\|367497
NZ_CP029149.1\|WP_160223737.1\|272204_272834_-\|ParA-family-protein	unknown	unknown	gnl\|CDD\|349760
NZ_CP029149.1\|WP_160223739.1\|274258_274639_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|275394
NZ_CP029149.1\|WP_160223734.1\|271060_271417_-\|DUF4134-domain-containing-protein	unknown	unknown	gnl\|CDD\|372636
NZ_CP029149.1\|WP_120489677.1\|289467_290325_-\|YihY/virulence-factor-BrkB-family-protein	unknown	unknown	gnl\|CDD\|377085
NZ_CP029149.1\|WP_120488707.1\|285372_286029_+\|carbonic-anhydrase	unknown	unknown	gnl\|CDD\|238448
NZ_CP029149.1\|WP_160223742.1\|277050_278571_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|240604
NZ_CP029149.1\|WP_160223746.1\|283477_284644_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|240612
NZ_CP029149.1\|WP_160223747.1\|287317_287983_-\|DUF2807-domain-containing-protein	unknown	unknown	gnl\|CDD\|371327
NZ_CP029149.1\|WP_120488706.1\|286156_287233_+\|ketoacyl-ACP-synthase-III	unknown	unknown	gnl\|CDD\|238426
NZ_CP029149.1\|WP_160223733.1\|270761_271058_-\|DUF4133-domain-containing-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_160223748.1\|288094_289027_-\|rRNA-pseudouridine-synthase	unknown	unknown	gnl\|CDD\|224108
NZ_CP029149.1\|WP_160223740.1\|275863_276037_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_160223735.1\|271458_271935_-\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP029149.1\|WP_160223743.1\|278560_280765_+\|peptidase-domain-containing-ABC-transporter	gnl\|CDD\|225183	COG2274, SunT, ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms].	0
NZ_CP029149.1\|WP_120489677.1\|289467_290325_-\|YihY/virulence-factor-BrkB-family-protein	gnl\|CDD\|377085	pfam03631, Virul_fac_BrkB, Virulence factor BrkB. This family acts as a virulence factor. In Bordetella pertussis, BrkB is essential for resistance to complement-dependent killing by serum. This family was originally predicted to be ribonuclease BN, but this prediction has since been shown to be incorrect.	4.87678e-33
NZ_CP029149.1\|WP_160223744.1\|280754_282059_+\|HlyD-family-efflux-transporter-periplasmic-adaptor-subunit	gnl\|CDD\|130902	TIGR01843, Hemolysin_secretion_protein_D_plasmid, type I secretion membrane fusion protein, HlyD family. Type I secretion is an ABC transport process that exports proteins, without cleavage of any signal sequence, from the cytosol to extracellular medium across both inner and outer membranes. The secretion signal is found in the C-terminus of the transported protein. This model represents the adaptor protein between the ATP-binding cassette (ABC) protein of the inner membrane and the outer membrane protein, and is called the membrane fusion protein. This model selects a subfamily closely related to HlyD; it is defined narrowly and excludes, for example, colicin V secretion protein CvaA and multidrug efflux proteins. [Protein fate, Protein and peptide secretion and trafficking].	7.15808e-21
NZ_CP029149.1\|WP_160223745.1\|282062_283397_+\|TolC-family-protein	gnl\|CDD\|224455	COG1538, TolC, Outer membrane protein [Cell envelope biogenesis, outer membrane / Intracellular trafficking and secretion].	1.95344e-41
NZ_CP029149.1\|WP_160223738.1\|272835_274290_-\|relaxase/mobilization-nuclease-domain-containing-protein	gnl\|CDD\|367497	pfam03432, Relaxase, Relaxase/Mobilisation nuclease domain. Relaxases/mobilisation proteins are required for the horizontal transfer of genetic information contained on plasmids that occurs during bacterial conjugation. The relaxase, in conjunction with several auxiliary proteins, forms the relaxation complex or relaxosome. Relaxases nick duplex DNA in a specific manner by catalyzing trans-esterification.	3.03941e-08
NZ_CP029149.1\|WP_160223737.1\|272204_272834_-\|ParA-family-protein	gnl\|CDD\|349760	cd02042, ParAB_family, partition proteins ParAB family. ParA and ParB of Caulobacter crescentus belong to a conserved family of bacterial proteins implicated in chromosome segregation. ParB binds to DNA sequences adjacent to the origin of replication and localizes to opposite cell poles shortly following the initiation of DNA replication. ParB regulates the ParA ATPase activity by promoting nucleotide exchange in a fashion reminiscent of the exchange factors of eukaryotic G proteins. ADP-bound ParA binds single-stranded DNA, whereas the ATP-bound form dissociates ParB from its DNA binding sites. Increasing the fraction of ParA-ADP in the cell inhibits cell division, suggesting that this simple nucleotide switch may regulate cytokinesis. ParA shares sequence similarity to a conserved and widespread family of ATPases which includes the repA protein of the repABC operon in Rhizobium etli symbiotic plasmid. This operon is involved in the plasmid replication and partition.	2.84475e-17
NZ_CP029149.1\|WP_160223739.1\|274258_274639_-\|hypothetical-protein	gnl\|CDD\|275394	cd13196, FERM_C_JAK, FERM domain C-lobe of Janus kinase (JAK). JAK (also called Just Another Kinase) is a family of intracellular, non-receptor tyrosine kinases that transduce cytokine-mediated signals via the JAK-STAT pathway. The JAK family in mammals consists of 4 members: JAK1, JAK2, JAK3 and TYK2. JAKs are composed of seven JAK homology (JH) domains (JH1-JH7) . The C-terminal JH1 domain is the main catalytic domain, followed by JH2, which is often referred to as a pseudokinase domain, followed by JH3-JH4 which is homologous to the SH2 domain, and lastly JH5-JH7 which is a FERM domain. Named after Janus, the two-faced Roman god of doorways, JAKs possess two near-identical phosphate-transferring domains; one which displays the kinase activity (JH1), while the other negatively regulates the kinase activity of the first (JH2). The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.	0.00710976
NZ_CP029149.1\|WP_160223734.1\|271060_271417_-\|DUF4134-domain-containing-protein	gnl\|CDD\|372636	pfam13572, DUF4134, Domain of unknown function (DUF4134). Based on Bacteroides thetaiotaomicron gene BT_0095, a putative uncharacterized protein As seen in gene expression experiments (http://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE2231), It appears to be upregulated in the presence of host or vs when in culture.	7.27446e-28
NZ_CP029149.1\|WP_120488707.1\|285372_286029_+\|carbonic-anhydrase	gnl\|CDD\|238448	cd00883, beta_CA_cladeA, Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes.	1.59933e-100
NZ_CP029149.1\|WP_160223742.1\|277050_278571_+\|hypothetical-protein	gnl\|CDD\|240604	cd12921, VKOR_4, Vitamin K epoxide reductase (VKOR) family in bacteria. This family includes vitamin K epoxide reductase (VKOR) present only in bacteria. VKOR (also named VKORC1) is an integral membrane protein that catalyzes the reduction of vitamin K 2,3-epoxide and vitamin K to vitamin K hydroquinone, an essential co-factor subsequently used in the gamma-carboxylation of glutamic acid residues in blood coagulation enzymes. All homologs of VKOR contain an active site CXXC motif, which is switched between reduced and disulfide-bonded states during the reaction cycle. In some bacterial homologs, the VKOR domain is fused with domains of the thioredoxin family of oxidoreductases which may function as redox partners in initiating the reduction cascade. This family also has a cysteine peptidase domain present at the N-terminus of the VKOR domain.	7.0377e-19
NZ_CP029149.1\|WP_160223746.1\|283477_284644_-\|hypothetical-protein	gnl\|CDD\|240612	cd12820, LbR_YadA-like, YadA-like, left-handed beta-roll. This group contains the collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins, including Moraxella catarrhalis UspA-like proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. These domains form a left handed beta roll made up of a series of short repeated elements. UspA1 and UspA2 are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric left-handed parallel beta-helices of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region.	1.255e-11
NZ_CP029149.1\|WP_160223747.1\|287317_287983_-\|DUF2807-domain-containing-protein	gnl\|CDD\|371327	pfam10988, DUF2807, Putative auto-transporter adhesin, head GIN domain. This bacterial family of proteins shows structural similarity to other pectin lyase families. Although structures from this family align with acetyl-transferases, there is no conservation of catalytic residues found. It is likely that the function is one of cell-adhesion. In Structure 3jx8, it is interesting to note that the sequence of contains several well defined sequence repeats, centred around GSG motifs defining the tight beta turn between the two sheets of the super-helix; there are 8 such repeats in the C-terminal half of the protein, which could be grouped into 4 repeats of two. It seems likely that this family belongs to the superfamily of trimeric auto-transporter adhesins (TAAs), which are important virulence factors in Gram-negative pathogens. In the case of Parabacteroides distasonis, which is a component of the normal distal human gut microbiota, TAA-like complexes probably modulate adherence to the host (information derived from TOPSAN).	1.04129e-38
NZ_CP029149.1\|WP_120488706.1\|286156_287233_+\|ketoacyl-ACP-synthase-III	gnl\|CDD\|238426	cd00830, KAS_III, Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.	2.17622e-79
NZ_CP029149.1\|WP_160223748.1\|288094_289027_-\|rRNA-pseudouridine-synthase	gnl\|CDD\|224108	COG1187, RsuA, 16S rRNA uridine-516 pseudouridylate synthase and related pseudouridylate synthases [Translation, ribosomal structure and biogenesis].	1.8754e-71

>NZ_CP029149.1|WP_160223740.1|275863_276037_+|hypothetical-protein
MNLNELKSTGVEIPRENLKSFKGGHSCRGEINLGIVSIRIGKRGCANGDAVHWFWED
>NZ_CP029149.1|WP_160223739.1|274258_274639_-|hypothetical-protein
MQKKDSEIKIRLEKSEKEEWQKFCKEQGITLTSLIVNSVKKRTWDSERRKAMAFIEKQVNLFAKVENNINQLAKYVNGQKFMTPQQANEFEMYLKAVKKLKQEQNEILMKTYHFIANDSENFKFGE
>NZ_CP029149.1|WP_160223738.1|272835_274290_-|relaxase/mobilization-nuclease-domain-containing-protein
MIVKILSSASNDFHGVKYNDKKMESGAGELMTMENFPDGFDENPKQDAVRNYFKSISKSEKVKKPQFHATISTKFQNHSKEELTEIGQNFMQEMGYGKQPYIIVFHNDTENNHIHIVSTRVDKSTGKKIDDSFEKLKSQRALQKVLAQLYGEQLDKDLEKLLRYRYGTTKQLALLLERSGFKMVQNKTDDTAFDILKNGVKQKTLEANQIVFHSKSDSKRAKQIKAFLEKYKSVYSNKVFKVIDNRETEGKPEEKTKRNIAPKIEFESELQYKMREMFGIDIVFHHKEGQKPFGYTLIDHKTQKVWKGSEIMKMNEIFDFTQEQLDKRLFEQMKDYNIFNGQQKQALLHFFNRYLTSEKIQDFMIFENKHRKNLEEYKKVREETFQAIKQPKQQTDISIFKGEDGRYYMVHQQYHHLHDLESLIGQTAYQNFVNPSSQKQERTYYQKDELSEALDEFWFEMMKNTGKGLDPAEEERKRKRKKRR
>NZ_CP029149.1|WP_160223737.1|272204_272834_-|ParA-family-protein
MIITFGTQKGGAGKTTLAIAFANYLSLQGKKLNVFDFDFQKSFYHKWAEDEALDLPQLYEVKVIGEDEKVVDFNTIMDMKESKEIFLFDLAGTIDDKYTHLLILSDYIVIPFEYSDVSAKSTLVFIELLSMIESEAQMIFVRSKYDKGYNYLNQEGMDAEISKYGKILENPIYKRNCLQNITTRKLTYEQKHSVKPTFDELMNFINATL
>NZ_CP029149.1|WP_160223736.1|271939_272218_-|hypothetical-protein
MPHYKLPFSIQLERKYNDINIDDFIKEWKENEKNRQERTIAIDNELHIELGKFNTFDINLNEIIDLGMRYALCKREFRRMMAQVIEQKNKKI
>NZ_CP029149.1|WP_160223735.1|271458_271935_-|hypothetical-protein
MGKSFLIIFGVYFLYYTGNILYDLFLKKEKIVETENNEQSFSLSELADQYQEKPISVEIEDVENIRTPQSFENEPYDFLSANEEPQSMEDLQKKYEDENQLNEMEHSETPQEKIEEKTTSIIDKPIKSLSIKDLLNDANTKVKMVANYEGQKVYNIQA
>NZ_CP029149.1|WP_160223734.1|271060_271417_-|DUF4134-domain-containing-protein
MNGTFKKLKGLKLANFKGVKREKVFILSLLLLSTTPVLAGGGAGAFTTAGNEVKKYWTPLKTFIQFVGGIVGLIGGLRIYNKWQNGDQDVNKEILGWGGACLFLTIVPTFVGSFFGLT
>NZ_CP029149.1|WP_160223733.1|270761_271058_-|DUF4133-domain-containing-protein
MGFYLYKGLKKPLVLFGLKDKYIYYGIGCVAVGLILSGVLGSFMGIWGTLLGLGLGALGFWSMYKIQDKKGLYNKTKNDDELHIFPKRFKITKFKSKN
>NZ_CP029149.1|WP_160223732.1|265382_265634_-|hypothetical-protein
MKYKKLIYTFSIFSMSILNAQVVKRLNDEAIVSQHKRMVFERWGDFRPYPKYNFLGIQTNLLTLPCGECGRLQGIEIIKWSRY
>NZ_CP029149.1|WP_160223731.1|264862_265339_-|hypothetical-protein
MEIQKQEAEKIKVEVDTIHKRNMQDFAHWDIYYCKCRPFVALYYKRMLRPLSEFPEAPQNYREWGFDNAEIYETLKFSGSIEKLQESLDLLKDKYHKSRTMDMPRGKRFLMYHETLLGWRKFQAELFSYNTKSELFFGLQKALDKFRKSRRIILQNPM
>NZ_CP029149.1|WP_160223742.1|277050_278571_+|hypothetical-protein
MSTFLFYELIRLNNYQIKKEDFDNEFMSHPDYPSLSAVKDTLDKFDIENIIAEFNNSHFNKLPNTFISSLKENSELILVKKKESSVLITNNFQHKKEIDISIFLENWSGLVIAVEKQKSTSKINIDIDNIIKKSFIIVITLILYFFYLNFDRYEFLYAFISLIGLCYCIEIYKTQHEINSKFIDKICSSKKENSCQMVMQEDRINIFGLKLSDMALLYFLTTTIFSLFLNKTQFIIILLSSLSIISVIYSIYIQFFKIRKTCKICLILIGIILSNSLICFLHFEFRFSTRVFLLCLIYFFIITPLYIYVNKIININKKLNHDNLINTRFKRNYDIFKRELFSSKQVNFKYKDLFFIGKKESKIHITLILNLECFFCKEAFYILKDIYLSNREYISLQIRFNFFNKPKLPEIGNFIKHLIYAYNKGENEFFSTFDKWYIQKYHFSKEESLINDFMEIEDISKENISEKLNDSPMLLINGYLFSQKYQIEDIYYFIEEIIKEYYNNDK
>NZ_CP029149.1|WP_160223743.1|278560_280765_+|peptidase-domain-containing-ABC-transporter
MINNKFPSYIQPDNKDCGPTCIKIIAKYYGVVLPLQYIRDLSETDREGTSLFGLSEAAEKIGFRSLGVNIDFNTLKNEVPLPCIVHWDSAHFVVVYKINKQNRVYISDPNYGLIDYTKEDFIKHWIGADNINENSKDGIALLLETTPNLYERENTNERDNKNNFYFLTKYITKYNKLIIQLFVGLFIGSLLNMTFPFLTQSIVDIGIHNQDLNFIYLILLAQIMLFLGKTSIEVIRSWILLHISSRINISIISDFFIKLMNLPINFFDTRLTGDIMQRINDHTRIEQLLTSTSLNTLFSIVNLLTFSIILLFYNYKIFIIYLIGGLIYIIWILFFLKKRKELDYKKFSQVSNEQSKVIELINGMQEIKMNNAERQKRWDWEYLQIRLFKLKIKSLSLEQIQSVGGNFINQIKDIFISFFSSQLVLNGDLTLGMMLSVQYIIGQLNNPLLQVIDFIKQYQDAKISLERLNEIHNKDDEEYHDKEYISEIPEGDLNLKNISFRYNGSDNYIFENLNINIPYKKTTAIVGTSGSGKTTILKLLSRFYEPNSGEVKVGNINISNISIKLWRKKCGVVMQEGYIFNDTIAKNIAIGEETINKERLRNSVKIANIKDFIEELTLSYNTKIGNEGIGISGGQKQRLLIARAIYKSPDYIFLDEATSALDANNENLIMNNLEQLFKDKTVVIIAHRLSTVKNADKIIVLNKGKIVEEGNHTELVAKKGEYYRLIKNQLELGN
>NZ_CP029149.1|WP_160223744.1|280754_282059_+|HlyD-family-efflux-transporter-periplasmic-adaptor-subunit
METKKDILNNTELRSENVQDILNKPPHWMIQWGNTLILIIFIIIIFMSYIIKYPEFINAPIIISSQNPPEKIEARISSKIEKILIQDQQKVQKGDILIVLQSTANYQDILALKDIVNSVNTNDIVNFPLSKTSQFRLGELQGDYNNFAKVLTDEILFTNLKPYAPDDIAISQNINENKNQLNILKQQLNLENAKYSLTKKNYERASTLFEQGVISKMEFENERLKFLQAQQSIEGVKMSISQLEDGAKNLQKSKKNVNINSIKDRTNYSTQSLYLLEQLRKSITQWEQNYLLTSSTDGIVSFQNFLGINQHISAGENIISIMPNEKEGIIGRMNIPSTNSGKIAIGNKVLVKLDNYRYQEFGIIEGQVKNISLTPDKDGNYYAYIILPKGLKTSYNKDIIFDKEMKGSADIVTQDLRLIERFLYQIRKLLGYQT
>NZ_CP029149.1|WP_160223745.1|282062_283397_+|TolC-family-protein
MKKYIVFGILCLPLVSFSQKKWTLQEAIDYATKNNLQIIDKEISLKIEENNLQITKNERLPSVAGNMSNQLRFGQTQGFQGGIGRNDNFNNDLNVSANILLYNGGRLQKQAIKKGYDVEIAQHNVALLKENIALQIIQQYLSVLLQKEIVKIYESSVENAQKGYQRAKITTEVGTTAQTTLAEAQSALAKENQNLNQSKIEVQKALFMLSQTLQLNDYHSFDIEYWSPSEELPTNLHSLESVLTQIREKHPLILSAQSQVKSAEAQTEVVKTAFLPSISLSAGLGSFYYNSLVTDITGVDNLGNIIKEKALFDQYKTNFYQQVGVSVNIPIFNKGNTKLQVEQAKINEVMAKNQLKIQEQQLLQQIQKVFFDMESHYQTYLSAQETEKSTQLALDFAQKSYEAGRTSIYDLHIARNNYVSAKSSTIQAKYNYIFSQKILDFYRK
>NZ_CP029149.1|WP_160223746.1|283477_284644_-|hypothetical-protein
MKHKITLFALLGTTLGFSQDYSGRVGINTETPNATLEVKGSPNDTEVIDGFIPPKITFSQITAKTNYNHHQTGALIYITDATNSEGIYNHQNQFIRTQGYYYWNGMTWRPLKGKDGELVRIETNTNRYGWGLPYRLNNPHNYDTIGEYAVDFSLSQVPTSRTGEQYGATGRASFAIGTHTIASGGYSFAHGERAFATGGYSYAGGIGTKATNFASHAEGQVTTASGWASHSEGYNTIADGTSSHAQGNSTIANSFAEHSRGTYNFSPTPYSKTSFDKRDLIESVGGGTGFISTGVYHRTNLFERYKSGAFKYNAQELNSANIPNASKGFHASDLNGKLNYHNGNEWETYITMKFADTEPNTAKKGDLYFNTQLNTYFAYDGTSWRSLW
>NZ_CP029149.1|WP_120488707.1|285372_286029_+|carbonic-anhydrase
MDSYATIFENNKKWVEKKLSEDKDFFKKLNKNQQPDFLYIGCSDSRVTAEELMGLGPGEVFVHRNIGNVINTLDMSSTAVIQYAVEHLQVKHIIVCGHYNCGGVKSAMTAKDYGLLNPWLRTIRDVYRLHQEELDAITTEKQKYRRLVELNVQEQCINVIKMACVQESYLEHKYPIVHGWVFDLKSGKLIDLDINFEKILKDIQKIYNLTGTDWFKYH
>NZ_CP029149.1|WP_120488706.1|286156_287233_+|ketoacyl-ACP-synthase-III
MPSTVIIGSGRYIPQNIISGKDFYSSEFYDENGQKIEKTNEEIVSKFIEITEIANRRYVDSDQLNSDIAAKASELAIQDAGIDKESLDYIISATNFGDIDENHQQSFMPSLSALVKHKLGIRNPKCVNYDMIFGCPGWVEGMILANVLIKSGRAKNILVVGSETLSRATDPYDRDKMIFADGAGAVVVSASDEEGVGIIADNTQCFNEEEIDYLKNGCSLNPNTDQNQRFVRMKGRKIYEFALKNVPVAIKDTIDKAGLSLTDIDKILIHQANAKMDHAIISRLHKLYNIKEYSDDLTPMTVHEYGNTSVACIPTMYDLIIKGEFSGHSFKDGSNIVLTSVGAGMNINAIVYRFPTKK
>NZ_CP029149.1|WP_160223747.1|287317_287983_-|DUF2807-domain-containing-protein
MKKLFAVLLGLASLWNFAQDTRMVGEFSSLKAYDGIKVDLVKSRQGKVEIYGDDNGDVEVVNKNGELKIRMKTLKLLQGSKVRVKVFYDDLNAIQASQGAIILSDDTLKSEMLKLTANEGSKIELKINSSVLDVKGNSGGTLSLQGKANTQSIVVNSGAVFNGKNMDGDNVSVTANAGGEAYVYAEKSVKATTRAGGTIEVYGNPKNRDTKKFVGGSISFK
>NZ_CP029149.1|WP_160223748.1|288094_289027_-|rRNA-pseudouridine-synthase
MNGRGSGKSGRPRLNKDGDTRGGRKPNSFDTRKKYEKGDLKFKKKPFSRFSDDPEKVKSFVQKRKLAKIDKDLHKDTIRLNKYIANSGICSRREADKLIEQGLVEVNGAVVTEMGYQVQKSDRVYFDGQPITPEKSVYVLLNKPRGYISTTKDEKARKTVMDLVANASPYRLFPVGRLDRSTTGVILLTNDGHMTKKLTHPSFNIKKIYHIVLDRKLSSEDLQTIAKGVRLEEGVAVVDHISFIEGKPRNEVGIEIHIGWNRVVRRIFQKMGYEVESLDRVMFAGLTKKNIKRGHWRILTELEVNNLKML
>NZ_CP029149.1|WP_120489677.1|289467_290325_-|YihY/virulence-factor-BrkB-family-protein
MFEIYIKGIFQNKLGKLAAAISWSFFLSLFPFILFLISLLPHLPHYERLMFYIFEILLPRIMPENILPDVTYYIKDILLPHRKGLNAMTIILALIFGTNGTYSLIRGFNENTTLRRGFIKEYFISLGVTIAFIALIILTFLGIYYSEIVLKLFTPSYDISWFVQNLSRIIGFISFPIFYLMLLSLFYWVGCLSISRWVQALPGAVFTTILFVLVTYFFAIYLKNFARYNLLYGSIGSIIVVMIWVNINIILLLLGNELNIAIRNIRLEKELAQTASSEKEKHFND

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Crispr_ID: NZ_CP029149_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP029149_2

355921-356026

Orphan

Consensus_repeat	Method
TTCTATAGTATTTTGAGGTAACACTTTTGCT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP029149_2

>merge|NZ_CP029149|2|355921-356026|CRISPRCasFinder
TTCTATAGTATTTTGAGGTAACACTTTTGCTCGTAGAACAGATTTAGGAGTATTAGGTTCTGTATTTTTAGTTTTTTCTATAGTATTTTGAGGTAACACATTTGCT

>NZ_CP029149|2|2|355921-356026|CRISPRCasFinder
TTCTATAGTATTTTGAGGTAACACTTTTGCT	CGTAGAACAGATTTAGGAGTATTAGGTTCTGTATTTTTAGTTTT
TTCTATAGTATTTTGAGGTAACACATTTGCT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP029149.1\|WP_160223772.1\|351693_353898_-\|bifunctional-(p)ppGpp-synthetase/guanosine-3',5'-bis(diphosphate)-3'-pyrophosphohydrolase	unknown	unknown	gnl\|CDD\|223394
NZ_CP029149.1\|WP_160223774.1\|357810_359181_-\|restriction-endonuclease-subunit-S	unknown	unknown	gnl\|CDD\|341135
NZ_CP029149.1\|WP_120488661.1\|345653_346346_-\|16S-rRNA-(uracil(1498)-N(3))-methyltransferase	unknown	unknown	gnl\|CDD\|236959
NZ_CP029149.1\|WP_120489676.1\|344861_345539_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_120488660.1\|346364_347771_-\|alkaline-phosphatase	unknown	unknown	gnl\|CDD\|224699
NZ_CP029149.1\|WP_160224673.1\|349512_350436_-\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|213236
NZ_CP029149.1\|WP_160223778.1\|367147_368011_-\|ATP-synthase-F1-subunit-gamma	unknown	unknown	gnl\|CDD\|376304
NZ_CP029149.1\|WP_160223779.1\|369662_370199_-\|ATP-synthase-F1-subunit-delta	unknown	unknown	gnl\|CDD\|365949
NZ_CP029149.1\|WP_160223768.1\|337259_339236_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|227112
NZ_CP029149.1\|WP_160223771.1\|350501_351665_-\|Na+/H+-antiporter-NhaA	unknown	unknown	gnl\|CDD\|377746
NZ_CP029149.1\|WP_160223776.1\|362998_364360_+\|D-alanyl-D-alanine-carboxypeptidase/D-alanyl-D-alanine-endopeptidase	unknown	unknown	gnl\|CDD\|224938
NZ_CP029149.1\|WP_160223777.1\|364382_365546_+\|HAMP-domain-containing-histidine-kinase	unknown	unknown	gnl\|CDD\|223715
NZ_CP029149.1\|WP_160223780.1\|370200_370695_-\|F0F1-ATP-synthase-subunit-B	unknown	unknown	gnl\|CDD\|184695
NZ_CP029149.1\|WP_120488649.1\|368065_369643_-\|F0F1-ATP-synthase-subunit-alpha	unknown	unknown	gnl\|CDD\|236448
NZ_CP029149.1\|WP_160223770.1\|343758_344850_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_160224674.1\|359167_361429_-\|N-6-DNA-methylase	unknown	unknown	gnl\|CDD\|280533
NZ_CP029149.1\|WP_160223775.1\|361455_362856_-\|tRNA-uridine-5-carboxymethylaminomethyl(34)-synthesis-GTPase-MnmE	unknown	unknown	gnl\|CDD\|235392
NZ_CP029149.1\|WP_160223769.1\|339397_343678_+\|cobaltochelatase-subunit-CobN	unknown	unknown	gnl\|CDD\|376805
NZ_CP029149.1\|WP_120488651.1\|365636_366977_-\|HlyC/CorC-family-transporter	unknown	unknown	gnl\|CDD\|224173
NZ_CP029149.1\|WP_120488659.1\|348183_349497_-\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|378925

Protein	Function_ID	Function_description	E-value
NZ_CP029149.1\|WP_160223772.1\|351693_353898_-\|bifunctional-(p)ppGpp-synthetase/guanosine-3',5'-bis(diphosphate)-3'-pyrophosphohydrolase	gnl\|CDD\|223394	COG0317, SpoT, Guanosine polyphosphate pyrophosphohydrolases/synthetases [Signal transduction mechanisms / Transcription].	0
NZ_CP029149.1\|WP_160223774.1\|357810_359181_-\|restriction-endonuclease-subunit-S	gnl\|CDD\|341135	cd17246, RMtype1_S_SonII-TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Shewanella oneidensis MR-1 S subunit (S.SonII) TRD2-CR2. This model contains Shewanella oneidensis MR-1 S subunit (S.SonII) TRD2-CR2 and similar TRD-CR's. S.SonII recognizes 5'... GTCANNNNNNRTCA ... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases. S.SonII TRD1-CR1 does not belong to this subfamily.	5.50932e-16
NZ_CP029149.1\|WP_120488661.1\|345653_346346_-\|16S-rRNA-(uracil(1498)-N(3))-methyltransferase	gnl\|CDD\|236959	PRK11713, PRK11713, 16S ribosomal RNA methyltransferase RsmE; Provisional.	1.77175e-62
NZ_CP029149.1\|WP_120488660.1\|346364_347771_-\|alkaline-phosphatase	gnl\|CDD\|224699	COG1785, PhoA, Alkaline phosphatase [Inorganic ion transport and metabolism].	7.65859e-94
NZ_CP029149.1\|WP_160224673.1\|349512_350436_-\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|213236	cd03269, ABC_putative_ATPase, ATP-binding cassette domain of an uncharacterized transporter. This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.	3.53535e-104
NZ_CP029149.1\|WP_160223778.1\|367147_368011_-\|ATP-synthase-F1-subunit-gamma	gnl\|CDD\|376304	pfam00231, ATP-synt, ATP synthase.	3.66632e-125
NZ_CP029149.1\|WP_160223779.1\|369662_370199_-\|ATP-synthase-F1-subunit-delta	gnl\|CDD\|365949	pfam00213, OSCP, ATP synthase delta (OSCP) subunit. The ATP D subunit from E. coli is the same as the OSCP subunit which is this family. The ATP D subunit from metazoa are found in family pfam00401.	8.52325e-46
NZ_CP029149.1\|WP_160223768.1\|337259_339236_+\|TonB-dependent-receptor	gnl\|CDD\|227112	COG4771, FepA, Outer membrane receptor for ferrienterochelin and colicins [Inorganic ion transport and metabolism].	2.58023e-70
NZ_CP029149.1\|WP_160223771.1\|350501_351665_-\|Na+/H+-antiporter-NhaA	gnl\|CDD\|377746	pfam06965, Na_H_antiport_1, Na+/H+ antiporter 1. This family contains a number of bacterial Na+/H+ antiporter 1 proteins. These are integral membrane proteins that catalyze the exchange of H+ for Na+ in a manner that is highly dependent on the pH.	0
NZ_CP029149.1\|WP_160223776.1\|362998_364360_+\|D-alanyl-D-alanine-carboxypeptidase/D-alanyl-D-alanine-endopeptidase	gnl\|CDD\|224938	COG2027, DacB, D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 4) [Cell envelope biogenesis, outer membrane].	6.9839e-55
NZ_CP029149.1\|WP_160223777.1\|364382_365546_+\|HAMP-domain-containing-histidine-kinase	gnl\|CDD\|223715	COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms].	1.08605e-24
NZ_CP029149.1\|WP_160223780.1\|370200_370695_-\|F0F1-ATP-synthase-subunit-B	gnl\|CDD\|184695	PRK14471, PRK14471, F0F1 ATP synthase subunit B; Provisional.	1.88222e-56
NZ_CP029149.1\|WP_120488649.1\|368065_369643_-\|F0F1-ATP-synthase-subunit-alpha	gnl\|CDD\|236448	PRK09281, PRK09281, F0F1 ATP synthase subunit alpha; Validated.	0
NZ_CP029149.1\|WP_120488659.1\|348183_349497_-\|ABC-transporter-permease	gnl\|CDD\|378925	pfam12698, ABC2_membrane_3, ABC-2 family transporter protein. This family is related to the ABC-2 membrane transporter family pfam01061.	6.92222e-31
NZ_CP029149.1\|WP_160223775.1\|361455_362856_-\|tRNA-uridine-5-carboxymethylaminomethyl(34)-synthesis-GTPase-MnmE	gnl\|CDD\|235392	PRK05291, trmE, tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE.	0
NZ_CP029149.1\|WP_160223769.1\|339397_343678_+\|cobaltochelatase-subunit-CobN	gnl\|CDD\|376805	pfam02514, CobN-Mg_chel, CobN/Magnesium Chelatase. This family contains a domain common to the cobN protein and to magnesium protoporphyrin chelatase. CobN is implicated in the conversion of hydrogenobyrinic acid a,c-diamide to cobyrinic acid. Magnesium protoporphyrin chelatase is involved in chlorophyll biosynthesis.	1.10307e-172
NZ_CP029149.1\|WP_120488651.1\|365636_366977_-\|HlyC/CorC-family-transporter	gnl\|CDD\|224173	COG1253, TlyC, Hemolysins and related proteins containing CBS domains [General function prediction only].	4.24597e-137
NZ_CP029149.1\|WP_160224674.1\|359167_361429_-\|N-6-DNA-methylase	gnl\|CDD\|280533	pfam02384, N6_Mtase, N-6 DNA Methylase. Restriction-modification (R-M) systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The R-M system is a complex containing three polypeptides: M (this family), S (pfam01420), and R. This family consists of N-6 adenine-specific DNA methylase EC:2.1.1.72 from Type I and Type IC restriction systems. These methylases have the same sequence specificity as their corresponding restriction enzymes.	1.11078e-30

>NZ_CP029149.1|WP_160223772.1|351693_353898_-|bifunctional-(p)ppGpp-synthetase/guanosine-3',5'-bis(diphosphate)-3'-pyrophosphohydrolase
MAYDLEKESKEILARYKDLISNTYRALDEDKNRLIRKAFDIALDAHKDQRRKTGEPYIYHPIAVAKIVAEEIGLGATSIACALLHDVIEDSEYTYEDLKRLFNEKIADIVRGLTKISGMANQNLSIQSENYRKLLLTLSEDFRVILIKIADRLHNMRTLDSMAPDKQKKIASETAYIYAPLAHRLGLYNIKSELEDLSLKYNNSEVYYEIADKLELAREHREKYIEEFKTEVSEQLAKEGLNFSIKGRAKAISSIYRKMLKQGVSFEEVYDNYAIRIIYKSDIKNEKFIAWKIYSIVTDLYHSNPSRMRDWITQPRSTGYESLHLTVLGPDKKWIEVQIRSERMDDIAEKGVAAHYKYKEGFKASSEDRNLEGWIKEIRYILEHQQSLSTTDFIDNIKLNLYSKDVFVFTPKGDVKTLPRGASALDFAFSVHSGLGMKCIGAKIHGKLVPISYILQNGDQIEILSSQNQKPKTDWLDFVITSKAKSKIKAFLNAEKTALVDEGKEILQRKLRHAKLNFNDNEINKMQKFFGLKTSQELFLGFQDGSLDAASIRKYIESKNVLSNIFSRFRKSPSKQTAVEDQPDKNLNLIVFGKDEEKLDYSFAKCCTVLPGDKIFGFVTISEGVKVHNENCPNAVNLRAQYDYRVIRAKWVNEENFKNRVKIELEGLDRMGMINDITQVITNAMHLDMKGMSIDSNNGVFSGVIHLEVKNKSQLEETLKKLKKIEGLSKVKRA
>NZ_CP029149.1|WP_160223771.1|350501_351665_-|Na+/H+-antiporter-NhaA
MKLTRYFKNFFNSSQSSGIILILCVIASLLTANSSFGEQFQALLDAEVGTEVFHLKYSVATWVNDGLMAVFFLLVGLEIKREIIEGELSNFKNASLPIFAALGGMMIPAIIYSFFNYGTPYAGGWGIPMATDIAFSLAIVSMLGNRVPPSIKIFLAALAIVDDLGAIVVIAVFYTESLHWLYLLLSLGIVVLLVLLNYFKVTKHIYYLVPGVFLWYFMHHSGIHATIAGVLLAFTIPTNVSRVKISPLEKLEQKLHFPVNYMIMPVFALANTNIMFKEGMVDGLFTSMGLGIIVGLFLGKVVGVCSFCFIAIKTKISALPQNSSWGQMLGVGFLAGIGFTMSIFIAMLSFKDAFHQSEAKFAILLASIISAIAGFLILKRAGDGKEY
>NZ_CP029149.1|WP_160224673.1|349512_350436_-|ABC-transporter-ATP-binding-protein
MLVAKNLTKTYNGGQKIALKDFSIEVPEGCIYGLLGPNGAGKTTFIRMLNQIIKPDAGSISINGEALCLKHIREIGYMPEERGLYKNMSVGDQLIYFGELKGMSRKAALDEAKKWFERLNIDQWWKKKITELSKGMAQKIQFVVTVIHRPKLLILDEPFSGFDPVNANLIKEQIIRLKTEGTTIILSTHRMESVEEMCDFVALINNSQKVLDGKLFDVKERFKENRFSVEIFNINREMLAKFKEKYSLNISNTVDMGLPLSFEVSGEYEQSAILSDLMTVGDIRRFDEKIPSMNEVFISAVERKNPL
>NZ_CP029149.1|WP_120488659.1|348183_349497_-|ABC-transporter-permease
MRNIILITKREYLTQVKKKSFIILTVLTPLLIIAFGGLIGFMFSINKSTAIIEVSDQSGLFKDELKSTDDVVYRFISAPTEKSIKTNLETREKLSGILVIPKLEAQNFDRLEENTTLWVNDNIGFEAKKSIVWDLKSILQKQKIKALGLKANEMESITKKTFNLNVESINEDNKADTDLAFGVKTGLGMLLMYVTFMFILMYGVRVMRSVLEEKNNRVVEIIISSVKPFELMMGKIIGVTFVALTQFSIWIMMSVAGAVFFNASFYRLPMNLPSGEVQTGNTDPNIIISEVSHTLLEMNFPLIILVFILFFLLGYVFYSSIYAAIGSAVDNETETQQFTLIAVLPMMIGVYGSFSIINNPDGPMAFWLSIIPFTSPIAMVARIPYGVPAWQIAISLFLLLGAALLMVYAAGKIYRTGILMYGNKLSLKNLYKWYRSR
>NZ_CP029149.1|WP_120488660.1|346364_347771_-|alkaline-phosphatase
MDRRKFIKGTALFSGLLAVNPLDLLSAKSLDLPQKGKKAKNIIFMVSDGMSSGTLAMANLYSNRILGRNGNWMNLYLENKVSRALMDTASASSIVTDSAAASSAFGGGIRVKNGVLNIGANGEKHLPIWQKFKMKGKKAGCVTTVTITHATPAGFCINSQKRKAEPEIAEMYANIGFDVMMGGGDENFNPEKRADKKDVYALYKQKGYQIFKDRNDFKKVDKNKPILGVFNHGALPYSIDRSSNKELQSVPTLAEMAKVAIDQMKDHKQGFVLQVEAGKVDWAAHGNDVAALIHDQLAFDEAIKVVMDFAEKDGETLVIITTDHGNANPGTIYGSGANKGFDSIADFKYTNEFLLNEIKPDYTPNQVKEWVREVNGFALTDDEAKHIIGFYNGLEKEDGLYNYKKLPFKFFADIQKKYDSVGWISMDHSGDYVELAVYGPGMELLKPFVKNTDLHYLMLNAAGVENKF
>NZ_CP029149.1|WP_120488661.1|345653_346346_-|16S-rRNA-(uracil(1498)-N(3))-methyltransferase
MKIFYGKVFPQVEINEDEQQHILKVLRMKDGQSLSITDGKGNLAHGKLIIEGKKALLGVEDIQADLPAFTPSLHIAIAPTKNIDRTEFFVEKATEMGISEITFLQTDNSERKNINIEKIRKQAIAASKQSLRVHFPIVNDLVKLRDFLKTIDPEKTFVAHCDRSLVRIPIQELKVENRLTILIGPEGDFSTAEIEQLSTLGIRAVTLGSQRLRTETAGVYAAAFIYSKMK
>NZ_CP029149.1|WP_120489676.1|344861_345539_+|hypothetical-protein
MILNILIVFIIINTLIKLSFWKLWQVAIMGVLSAGFLLFAYTYAIEQSQVTIQQALENTKVLSNMAVLVSIEAGFCIGFCFLALRTLFLGKESRGYKILKWYPSLLIFPVLFYLLTQSIFYFSGADFFTTTTVLAIGVLLLIIGGAYGIKELLPEEDFRLEVHFLTSLFITILGLISTTNGNTIYVPKSEPMNFTALGLTFLLFIGMFILGFFINKIWWRIRKTK
>NZ_CP029149.1|WP_160223770.1|343758_344850_+|hypothetical-protein
MKIRLLSILSFISVCTFAQNNDIWTAFYNPDTDDIGFKNSKGEVMIKPRFRGLISARKFDKIIALMDDENFSRVYYMLKNGKTFGKDSTYIFDMTFDCESEGFIRFHDSKTDKVGMFNHEGKIVIPAKYSDLFPVKNGMTIALQGAYKEYWEKHNEHSGCNHWSWVGGKNVLINSKNEILVEDFPEPKSLDLYSSKVAEKPIKDENRINVLGKNGKYYSFVDNEKLFKNFIEKLIKNLNKEYLLKNSYKEIVYWDEEKGWISAPAKDFIEKNYTILSEKLKAYFSKKDYQLSDYTPLTEKIEKEFEHHYNNCGERDINRFPIFNLIISYYEKGKFSHQDHFNFIKTEEGIQFISCTIRNHTLK
>NZ_CP029149.1|WP_160223769.1|339397_343678_+|cobaltochelatase-subunit-CobN
MKNKKKILLAVFIAVLLSACWFVWSKWASPTRIALVNFPNYQVSNIALSNSDSFIKFVDVPLEEIDKLDGYDFVLTWGMGLRINDEQRETFLKIAEKVPTHFISVTSPENDITSLSETQLEEVDAYLNSANKKNYQNFARYVRTKINGKKLFATAPEKPAKSIGDAFFYLGEDNHFPTLKDFEAFLKKEKIYKEGKPKVAFITGIHDPFSGNRQHIDSIIVSLEKSGLNVYPFASFGKRIDFLKEINPDAVIYMPHGRVQMMDPEVTVEYLKEKNIPLFTPISIIQLEEEWKKNPMGMFGGFMGQTIVMPELDGALYPYALIAQEKSKDGFYMFKAMPERLKTFTQVVNNYLRLKEKQNAEKKVAIYYFKGYGENPLVAQGLETNASLYNFLKRLKAEGYTVDDLPATEEEFEKVLNLKGNIFLSSAQGAFDEYVKNGDPELIETTQYEKWLKGALSKDLYKKVMEKNGAAPYSYMGVTKDGKNYLAVSRVKFGNVVILPQPPAGISSDDQFKVVHGAKEIPPHAYIGTYLWTQHGFKADAMIHFGTHGSLEFTPHKQVALDGDDWGDICIGAVPHFYYYTIANVGESIMAKRRTYASLVSYLNPAFTESDTRTAFNSLMDKINYYYKAKEEDHKRDLSLKIKADAVKMGFHRSLRLDSVLTKPYTEEEIDKLENFAEEIATEKINGQFYTMGEPYSSDKIQSTVLAMSTDPLAYSVAALDKLRGKVTDQQLKRKVFFTENYLNPAKNLVNQILAGREVTPELVAQVAGVPVSEIEKSREILTPKREMPFFLKKSMEKKGKGSAELSDIEKQLKAGKIPEGMPEFVAKKLMEKVKRGERLEPYNPGGKRTVKKGEAKTETKKPEIPKEVKEKAIAVLDIERTLKAVVDNKKALLESPEIEFKSFINALNGGYTPPSSGGDLVANPRAVPTGRNMYSVNAEMTPSELSWDRGVTLAKATIEEYKKKHKGAYPKKVAYTFWSSEFIETEGVSIAQALYMLGVEPVRDSFGRVVDVRLIPSKELGRPRIDVVIQTSGQFRDLAASRLFLLTKAVEMAANAKDDEFDNQVSAGTIEIEKQLVKAGVPPKRAREMSNYRIFGGQQGRYDTGTKEMMLSGDKWESTQDIAKTYIHNMGALYGSEKEWSQHEEGMFRAALSNTDVLIQPRQNNTWGALSLDHVFEFMGGMNAAIKDVTGKDPDAYLADYRNHKNMRMQELKEAVGVEAQATIFNPKYIKEMMKGKSSSAGQIAEIATNMFGWEATRPEVVDDAMWEELYQTYVEDKHNLGIKDFIHQKNSASLQTVTAVMLEATRKGMWKADAGKIAKLAMMHNDLVKENGAESSDFSAKNVKLQNYIAKKLPEAQATEYKGSLEKMKSGTTQVKDGKVLKKEENNTEQLKEKVSLNGLFIGGGILIVFIALLIYFKKKRKSD
>NZ_CP029149.1|WP_160223768.1|337259_339236_+|TonB-dependent-receptor
MLKLKISTALVIVLISVPLFGQRKTEKKKDSIKDIQEVVVTATRSLKKLKDVPIPVQVITSDEIKKSQSKDFQSFLENEFSGINFTYDGGMPNINMMGFGGKYILFLVDGQRLAGETFDNIDYDRIDLDNIERIEIIKGASSSLYGSNAIGGVINIITKNSQSPLDITAGYLYDTSINHKINFSAGTKQKWGSFSVSSFYKMREPYIIRGTEPVIDNSGVAKYPEINVAGFTNYAINPKLQFNISPKIDLTLTPGYYYSERNRGDNDSKKIRDKYYNYTGGLKANFKLTEDKNLSISGAFDRYDKFKYYRLLKQKEKDYENQIVRSTAEYNQTLFGKHTLVAGGEVLADRLLSFRFNDSGSAEKKQAETYTLFTQQDWVLSPSFTLVTGARLDHHSLFKNFFTFRLSGMYKLDNLMTLRGGYSGGFRSPTLKELYTNWFHPWGGGFQIMGNKNLKPETSDNYTVSVDFNLNKKLNLTFMTQYSSIKNKISNKWTANNDTIRYVNFSGRSDIIGSEVSATYRPNKHFKFGTSYSYYSIGQRRITEIRPHTLTFKAEYSSHKLYIPDVLISGKYISGSTLAEKDSAGNITTYWYSPYSLWWLKLSSQLPLNFSVVAGVSNLFNYKTPTADFYSPISPGRTYYLGVRWNFNMKKKENDDTL
>NZ_CP029149.1|WP_160223774.1|357810_359181_-|restriction-endonuclease-subunit-S
MKTYKKLKFVGFSNIESWSASFLFGTINKFNRKYRVLKISQLLVKNNESIIIEDEKLYKRVTVKINANGVVLRDEEYGKNIGTKRQFIAKEGQMIVSKIDARNGAFGLIPSELDGAIVTNDFPLFDIDHHLVNKNYLILLAKTNLFVGFAKSCSSGTTNRQRMDMDKFLTLEIPLPSISEQETIVKNYYDKITQATTYEQQAETLEKNIESYLFESLGIEQKTEQKTKKKGLQFVEFYKMDFWGVDKIKLDKELHSSRYEVTSIGDFPELLVTCFRGKSPKYTEVSSKFILNQKCNRWNSIDFSFVKSIDEDWYNNIDEDFFTKEGDILVNSTGEGTIGRATYITKNYEGLIYDSHMLLLRLNRSIYNPILFVDLFNSSYIQTQIDKIKSAQATKQTELGINNLLKIRIPILSNLQVQQTIITQIDTYKNEIKILRERATLLKQQAEQEFEQTIFS
>NZ_CP029149.1|WP_160224674.1|359167_361429_-|N-6-DNA-methylase
MEVQIKDNKIFAPLKDKWLVLKPEEKVRQEYICRLVNSYGFDLKQMDQDSKVQGIYLNYSILIWKNKNSKINNESPLIVIQCKADSVIIKKEDYFKGLDFSREIGAKFFVATNFKQTKIYSKIYRTDSENVEEILDIPNKEEAQNIQEIEKLLNKNNTFQRENFTKTLDKCHSIIRNNDKLSPEAAFDEISKILFIKTIYERDNSKNQIFSLDIYKKEKIDFEKYRFNERKDFYQFLFEQTKKSYIDDDLFEPTEIIRIRENSFEAIVKELEIYNLSTTSDDVKGIAFEQFLGKTFRGELGQFFTPRTIVDFMVEVLDPQETETICDPCCGSGGFLIKAFEYVRAKIEAKVQQEKELIKQEYYTETYEKLSDAEKEKIDDRVNKFFSQLNEELNINNDKSRIRTLSYDCIFGTDANPRMSRTAKMNMIMHGDGHGGVHHNDGLLNVNGIFENRFDVILTNPPFGARVEKSLKITEADKYTDEERIKKYQKRYGDEYNKALKQVNNNIGKPLVSLYKMGAMSTLTEVLFIERCLNLLKPGGRMGIVLPEGVLNNSNLQKVRDYVESKAKILLIVSIPQDVFIASGATVKPSLLFFKKFTEEEALQYASIKSKATITIEAKYAEEVANIQQKLAKKGKEALPAEEEKQLKTEKKNIEAKKEREIKAIVKEEFNYTIPIAEVEKAGISTTGARIDNELEPLAKEFKKYSSENHLWGKLTESVQYDVKGEFVYRIQIADKEVGEPEIFYQKSKYENL
>NZ_CP029149.1|WP_160223775.1|361455_362856_-|tRNA-uridine-5-carboxymethylaminomethyl(34)-synthesis-GTPase-MnmE
MNQDTICALATANGVGAIGIIRISGEDAVSITNKIFEGKDLEAVKTHTVHYGFIKDNDEVIDEVMVSVFYAPRTFTAENSVEISFHGSPHIAKRILEALINNGARMAKAGEFTMRAFMNGRIDLSQAESIADLIASENEAARKMALNQLKGGISQEISILRNDLLNFTSLIELELDFSEEDVEFADRSALNQLLQNLKTKLQSLIDSFQYGNAMKNGIDVAIIGKPNAGKSTLLNALLKEERAIVSDIAGTTRDTIEEVLHIKGTAFRFIDTAGIRETVDKIEEIGVKKAKEKISTAKILLYLYDEFDSTAEEVISFIKEIYREDLKVILLHNKIDKLVDREEPTLNSFDAQLKAELVPYYTDTIMGISARDNINIELLKAELANYVEELKTEENAVVITNQRHYEALQKSFNSVQKVEEAVSMGIQTELLAYELRTALEHLGEISGEFTNDEVLGNIFSKFCIGK
>NZ_CP029149.1|WP_160223776.1|362998_364360_+|D-alanyl-D-alanine-carboxypeptidase/D-alanyl-D-alanine-endopeptidase
MNRFSLWAVCISAFSFAQNISQKLDKSISNLLNTNEAYSANISFFVSDSKGNLIYEYQGNKGLSTASTQKIFSAGAALETLGSNYRYTTTVSYSGKVESGNVSGDIIITSNGDPTLGSWRYEGYKPEDFKQKLLSSLTQNNISKISGNIIIDDSWFDLQTIPGGWAWDDLGNYYGAGVWGVNWRENQFDLNIKGSEIQSANIPLPNLHWASELKAKGSTDQSLIFTAPHSEVALINGNLPSGKLMTVSGATPNPPLSLGYEVKSWLKEAQISFSGEILTSSGEKFKGNASPLPSSSTKILEYYSPTLDKIVFWFLRKSVNLYGETFIKTIAKEKTGESNYKTGIALLKNFWASKAGIHKAMINFADGSGLSPQNYVSAKAEVQALLWAKKQNWFNAFYDALPTLNGMKMKSGTIRNTKSFAGYHNGYTFSIIINNYQGNNATEALYKVLNHLK
>NZ_CP029149.1|WP_160223777.1|364382_365546_+|HAMP-domain-containing-histidine-kinase
MKRRLYLSKFNVWLTYIFFTGIVSAIVVYSIFLVKELRARETNRMGIFVKAMQLLQENPTSISPDTQDLILSILEENNQLPVIVTDSRKRPIISEGTFRNIPEDIIKDKNHLKTYIQQMESNYPPFEIKLANNETQLVFYDNSALLNNLQYYPYFLGVFILSYLIVSIWFMQTMKRRDEGFLWAGLAKETAHQIGTPLSSMIGWTEILKLENPNSTGIDEIEKDILRLKTISERFSKIGSIPELKDYNLSETLRLNFDYLKSRISAKINFTLSLPEQEILIPHNRILFSWVIENLVKNAVDAMKGIGSLHISLYQKNHSIFMDFKDSGCGMTSKQAQRIFLPGYSTKKRGWGLGLSLAQRVIKTYHKGKISIAETEINKGTTFRIKL
>NZ_CP029149.1|WP_120488651.1|365636_366977_-|HlyC/CorC-family-transporter
MDDSVRILLALFLVILNGFFVAAEFSIVKVRYSQIQIKAAEGNPLAKQAEHIIKKLDAYLSATQLGITLASLALGWVGEAAVHSVIERLFLSFNIGLDETLLTTLSLVLSFLIITILHIVFGELVPKSIAIRKSEPTAMFIAYPLRIFTTLFQPFIWLMNSTSNGFLRLINIPPASDSDIHSTEELQLLVKQSADSGEIEEENYEIIKNAFDFTDHSAKQIMVPRQNIHSIDIEDPIDDILNTIMESGYSRIPVYEDSIDNIIGVLYTKEIIREYVKRSGNISHSDLRELMREAFFVVGSKKISDLLKVFQSKKMHLAIVIDEFGGTEGIITLEDILEELVGEIQDEEDDEEKIVEKVDENTYWVQAAQPLEEINEHLPEALPLSDEGDYNTLAGFILHELEDIPEENQEFNLLNYHFKIHKMQNKGVELVELIYQPPSDDSTNNQ
>NZ_CP029149.1|WP_160223778.1|367147_368011_-|ATP-synthase-F1-subunit-gamma
MANLKEIRGRITSISSTMQITSAMKMVSAAKLKKAQDAIVMLRPYSEKLQELIQNVNSSSNPDNISVYAQAREVKRVLFIAITSNRGLAGAFNSSVIKELNHQIALKEGVEVEVLTIGKKAFDAVKKLKEVYANHSAIYDNLTFDAVSSVAYSVMKDFVEGKFDEVYLIYNKFINAATQEVQAEKFLPISMPETEDVGVEKDYIFEPSRAEILDNLIPKSIKTQLFKAVLDSVASEHGARMTAMHKATDNAQALKSELVIYYNKARQAAITNEILEIVSGAEALKNS
>NZ_CP029149.1|WP_120488649.1|368065_369643_-|F0F1-ATP-synthase-subunit-alpha
MAEINPAEVSAILKQQLANFDTQSNIEEVGTVLTIGDGIARVYGLENVQYGELVKFSSDVEGIVLNLEEDNVGIALLGESKLVKEGDTVKRTNRISSIKVGEGLLGRVVDTLGNPIDGKGPITGDLYEMPLERKAPGVIYRQPVNEPLQTGIVAVDSMIPIGRGQRELIIGDRQTGKTTVAIDTILNQKEFYDAGEPVFCIYVAVGQKGSTVAQIVQTLADKGALAYTVVVAANASDPAPMQVYAPMAGAAIGEFFRDTGRPALIVYDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKVIADDEIAKQMNDLPESLKPVVKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGVRPAINVGISVSRVGGNAQIKSMKKVSGTLKLDQAQYKELEAFAKFGSDLDAATLSVITKGEKNVEILKQPVNSPLRVEDQVAMVYAGTENLLRNVPVRKVKEFMKEYVEFLRAKHPDTMAAIKAGKIDGDITSVLKAAANDIAAKYN
>NZ_CP029149.1|WP_160223779.1|369662_370199_-|ATP-synthase-F1-subunit-delta
MLTSKVARRYAQGLLDFAKESNQTQTIYTEMKDIIKVLSESKDLVRFLETPFIDYKKKLSVVQEIFKGFSPVSQNFVKLVISRGRESHLEEIAQEYINKINAENNVQKVTLTTATQLSSQSVDHILKSTTLVQGSQYELELIIKPEILGGYILRVGDQQIDASVKSKLNQIKKNFQLN
>NZ_CP029149.1|WP_160223780.1|370200_370695_-|F0F1-ATP-synthase-subunit-B
MELLTPSIGNIFWTAVVFLILVALLAKYAWKPILSAVNEREVSITDALNQAKLARKEMESLKADNERIVREAKIERDAILKEARELKDKIVSEAQDVAKAEGEKLIEQAKQTIQAEKAAAMADIKNQIGALSVGIAEQILKQKLDNSDAQNALVENYLNNSNHN

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Crispr_ID: NZ_CP029149_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP029149_3

632818-633007

Orphan

Consensus_repeat	Method
TAACATTAGAAGTATTCCAGTTACCAATAGGTTGATTAAA	PILER-CR

2 spacers

The CRISPR arrays of NZ_CP029149_3

>merge|NZ_CP029149|3|632818-633007|PILER-CR
TAACATTAGAAGTATTCCAGTTACCAATAGGTTGATTAAAGGATGTAGCTCCCCTAAACATATCTCTCATATCCGTAACATTAGAAGTATCCCAGTTACCAATAGGTTGATTAAAGGATGTAGCATTTTCAAACATATAATGCATTACGTTTACATTAGAGGTATTCCAGTTACCAATAGGCTGATTAAA

>NZ_CP029149|3|1|632818-633007|PILER-CR
TAACATTAGAAGTATTCCAGTTACCAATAGGTTGATTAAA	GGATGTAGCTCCCCTAAACATATCTCTCATATCCG
TAACATTAGAAGTATCCCAGTTACCAATAGGTTGATTAAA	GGATGTAGCATTTTCAAACATATAATGCATTACGT
TTACATTAGAGGTATTCCAGTTACCAATAGGCTGATTAAA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP029149.1\|WP_160223936.1\|644166_646935_-\|propanediol-utilization-protein	unknown	unknown	gnl\|CDD\|316139
NZ_CP029149.1\|WP_160223929.1\|628781_629636_+\|tail-fiber-domain-containing-protein	unknown	unknown	gnl\|CDD\|379398
NZ_CP029149.1\|WP_160223930.1\|629642_631706_+\|BACON-domain-containing-protein	unknown	unknown	gnl\|CDD\|271342
NZ_CP029149.1\|WP_160223937.1\|646939_647785_-\|T9SS-type-A-sorting-domain-containing-protein	unknown	unknown	gnl\|CDD\|275036
NZ_CP029149.1\|WP_120488476.1\|623304_624432_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_160223927.1\|621935_622631_-\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|276809
NZ_CP029149.1\|WP_160223931.1\|633609_634497_-\|tail-fiber-domain-containing-protein	unknown	unknown	gnl\|CDD\|379398
NZ_CP029149.1\|WP_120488467.1\|638298_640569_-\|aconitate-hydratase	unknown	unknown	gnl\|CDD\|235974
NZ_CP029149.1\|WP_160223934.1\|636675_638178_-\|glutamate--tRNA-ligase	unknown	unknown	gnl\|CDD\|234953
NZ_CP029149.1\|WP_160223933.1\|635404_636388_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_120488480.1\|620319_621081_+\|succinate-dehydrogenase/fumarate-reductase-iron-sulfur-subunit	unknown	unknown	gnl\|CDD\|181038
NZ_CP029149.1\|WP_120488474.1\|627367_628306_+\|ribose-phosphate-pyrophosphokinase	unknown	unknown	gnl\|CDD\|234929
NZ_CP029149.1\|WP_120488481.1\|618280_620293_+\|fumarate-reductase/succinate-dehydrogenase-flavoprotein-subunit	unknown	unknown	gnl\|CDD\|236054
NZ_CP029149.1\|WP_120488464.1\|642620_644015_+\|class-II-fumarate-hydratase	unknown	unknown	gnl\|CDD\|234779
NZ_CP029149.1\|WP_160223935.1\|640853_641975_-\|3,4-dihydroxy-2-butanone-4-phosphate-synthase	unknown	unknown	gnl\|CDD\|181774
NZ_CP029149.1\|WP_160223932.1\|634604_635390_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_160223928.1\|624860_627221_-\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|227122
NZ_CP029149.1\|WP_120488465.1\|642116_642392_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_120488479.1\|621451_621934_-\|6,7-dimethyl-8-ribityllumazine-synthase	unknown	unknown	gnl\|CDD\|187742
NZ_CP029149.1\|WP_120488477.1\|622717_623245_-\|adenine-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|235028

Protein	Function_ID	Function_description	E-value
NZ_CP029149.1\|WP_160223936.1\|644166_646935_-\|propanediol-utilization-protein	gnl\|CDD\|316139	pfam13583, Reprolysin_4, Metallo-peptidase family M12B Reprolysin-like. This zinc-binding metallo-peptidase has the characteristic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.	7.28109e-40
NZ_CP029149.1\|WP_160223929.1\|628781_629636_+\|tail-fiber-domain-containing-protein	gnl\|CDD\|379398	pfam13884, Peptidase_S74, Chaperone of endosialidase. This is the very C-terminal, chaperone, domain of the bacteriophage protein endosialidase. It releases itself, via the serine-lysine dyad at the N-terminus, from the remainder of the end-tail-spike. Cleavage occurs after the threonine which is the final residue of the End-tail-spike family, pfam12219. The endosialidase protein forms homotrimeric molecules in bacteriophages. The catalytic dyad allows this portion of the molecule to be cleaved from the more N-terminal region such that the latter can fold and presumably bind to DNA.	1.48498e-12
NZ_CP029149.1\|WP_160223930.1\|629642_631706_+\|BACON-domain-containing-protein	gnl\|CDD\|271342	cd14948, BACON, Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.	1.1168e-08
NZ_CP029149.1\|WP_160223937.1\|646939_647785_-\|T9SS-type-A-sorting-domain-containing-protein	gnl\|CDD\|275036	TIGR04183, hypothetical_protein, Por secretion system C-terminal sorting domain. Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.	3.71824e-13
NZ_CP029149.1\|WP_160223927.1\|621935_622631_-\|tetratricopeptide-repeat-protein	gnl\|CDD\|276809	sd00006, TPR, Tetratricopeptide repeat. The Tetratricopeptide repeat (TPR) typically contains 34 amino acids and is found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans. It is present in a variety of proteins including those involved in chaperone, cell-cycle, transcription, and protein transport complexes. The number of TPR motifs varies among proteins. Those containing 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accommodate an alpha-helix of a target protein. It has been proposed that TPR proteins preferentially interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes.	1.52152e-05
NZ_CP029149.1\|WP_160223931.1\|633609_634497_-\|tail-fiber-domain-containing-protein	gnl\|CDD\|379398	pfam13884, Peptidase_S74, Chaperone of endosialidase. This is the very C-terminal, chaperone, domain of the bacteriophage protein endosialidase. It releases itself, via the serine-lysine dyad at the N-terminus, from the remainder of the end-tail-spike. Cleavage occurs after the threonine which is the final residue of the End-tail-spike family, pfam12219. The endosialidase protein forms homotrimeric molecules in bacteriophages. The catalytic dyad allows this portion of the molecule to be cleaved from the more N-terminal region such that the latter can fold and presumably bind to DNA.	2.9543e-15
NZ_CP029149.1\|WP_120488467.1\|638298_640569_-\|aconitate-hydratase	gnl\|CDD\|235974	PRK07229, PRK07229, aconitate hydratase; Validated.	0
NZ_CP029149.1\|WP_160223934.1\|636675_638178_-\|glutamate--tRNA-ligase	gnl\|CDD\|234953	PRK01406, gltX, glutamyl-tRNA synthetase; Reviewed.	0
NZ_CP029149.1\|WP_120488480.1\|620319_621081_+\|succinate-dehydrogenase/fumarate-reductase-iron-sulfur-subunit	gnl\|CDD\|181038	PRK07570, PRK07570, succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated.	0
NZ_CP029149.1\|WP_120488474.1\|627367_628306_+\|ribose-phosphate-pyrophosphokinase	gnl\|CDD\|234929	PRK01259, PRK01259, ribose-phosphate diphosphokinase.	2.54703e-180
NZ_CP029149.1\|WP_120488481.1\|618280_620293_+\|fumarate-reductase/succinate-dehydrogenase-flavoprotein-subunit	gnl\|CDD\|236054	PRK07573, sdhA, fumarate reductase/succinate dehydrogenase flavoprotein subunit.	0
NZ_CP029149.1\|WP_120488464.1\|642620_644015_+\|class-II-fumarate-hydratase	gnl\|CDD\|234779	PRK00485, fumC, fumarate hydratase; Reviewed.	0
NZ_CP029149.1\|WP_160223935.1\|640853_641975_-\|3,4-dihydroxy-2-butanone-4-phosphate-synthase	gnl\|CDD\|181774	PRK09311, PRK09311, bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II.	3.24077e-142
NZ_CP029149.1\|WP_160223928.1\|624860_627221_-\|tetratricopeptide-repeat-protein	gnl\|CDD\|227122	COG4783, COG4783, Putative Zn-dependent protease, contains TPR repeats [General function prediction only].	4.74732e-08
NZ_CP029149.1\|WP_120488479.1\|621451_621934_-\|6,7-dimethyl-8-ribityllumazine-synthase	gnl\|CDD\|187742	cd09209, Lumazine_synthase-I, lumazine synthase (6,7-dimethyl-8-ribityllumazine synthase, LS), catalyzes the penultimate step in the biosynthesis of riboflavin (vitamin B2); type-I. Type-I LS, also known as RibH1, catalyzes the penultimate step in the biosynthesis of riboflavin in plants and microorganisms. LS catalyse the formation of 6,7-dimethyl-8-ribityllumazine by the condensation of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione with 3,4-dihydroxy- 2-butanone-4-phosphate. Subsequently, the lumazine intermediate dismutates to yield riboflavin and 5-amino-6-ribitylamino- 2,4(1H,3H)-pyrimidinedione, in a reaction catalyzed by riboflavin synthase synthase (RS); RS belongs to a different family of the Lumazine-synthase-like superfamily. Riboflavin is the precursor of flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) which are essential cofactors for the catalysis of a wide range of redox reactions. These cofactors are also involved in many other processes involving DNA repair, circadian time-keeping, light sensing, and bioluminescence. Riboflavin is biosynthesized in plants, fungi and certain microorganisms; as animals lack the necessary enzymes to produce this vitamin, they acquire it from dietary sources. Type II LSs are distinct from type-I LS not only in protein sequence, but in that they exhibit different quaternary assemblies; type-I LSs form pentamers. The pathogen Brucella spp. encode both a Type-I LS and a Type-II LS called RibH1 and RibH2, respectively. RibH1/type-I LS appears to be the functional LS in Brucella spp., whereas RibH2/type-II LS has much lower catalytic activity as LS. The pathogen Brucella spp. have both a type-I LS and a type-II LS called RibH1 and RibH2, respectively. RibH1/type-I LS appears to be a functional LS in Brucella spp., whereas RibH2/type-II LS has much lower catalytic activity as LS.	2.38648e-68
NZ_CP029149.1\|WP_120488477.1\|622717_623245_-\|adenine-phosphoribosyltransferase	gnl\|CDD\|235028	PRK02304, PRK02304, adenine phosphoribosyltransferase; Provisional.	2.36625e-74

>NZ_CP029149.1|WP_160223930.1|629642_631706_+|BACON-domain-containing-protein
MKKRLYILLGLLVSGLQYLTFAQSTPQQSITCKFGSPQITLKAGQLKVATWGGTYLFGCIPNQLDPSSTNGQYVALDEHAQNVAEAPTENGKIKYTPTHGSVIRLENQNRPLRNRNFTPLGFPNNPHSHKVGKIIYYLNHYWEGVEGNKWHLLDNAIIFEVYPEVLTLDYNAGSTTINVYSNGSWTSSGLSIAGESLTPSSSSVNGHTPVTYNYPENNTDRISNRTIYFKRENLNLTRTVKVVQNYKPKYLYSNILDVYGKEQSGTVPEEYKGKVNPGPERFFAWVTSPTKFRMRIKYNGGPIGSYTHPDPVLGDYDYEYDGKGDIIAYEYQLKENLTNADRKIDLEISFQKANGDWEPWEDVGLKNSNNTAVTQSHLQHKARRRWSKKYIGATEDAKDVSYVYQRLDHYKSLPSSYYKEQAGTWTTGLKNDNPLVTGYTEAGVGSGWKVPDEEDLKDLKIAGFIPNRPFLYTYDSPTRIPAADTKYNNWAINSSNTVLLDSEVFSKQKYGYGNAFYLYDKTGSMVWFPINGRIEYYRQSFFNLTEYSIDHKINLLGTHISNSSSTTETTDYYRYADYVTCYRNGQSEPQHYLKYSVDTRNLGNKFKLGIISTQNGVDIKDDQYISSYSLTESYGESRECTVTSSCYHNGPVFGPAPPAIQCGRWKDFYDYYSFTKNYQYTYRLTHD
>NZ_CP029149.1|WP_160223929.1|628781_629636_+|tail-fiber-domain-containing-protein
MKQKLFFAMLLTGVLASAQTDYQGKVGINTAEPKATLDLNPSTENAKVKSNASNEGLLIPRLSKERLAKVASTNLQESTLVYVNDVSYTGAETTIKNVKSKGFYFYNGTEWTAVIGAGASSSVKTLYTDDGEISAARTVTVKNSGSLVFKREAGNNNEAVDVQGMLKVTSIDMNSDRRLKREIQPITQPNSLSALRPVSYYWNVEGEKRGGNKDLQYGFIAQEIEQVYPHLVNTSSDGYKSVNYIQVIPLLVKELQESQAKLKDLEGRLEKLEGKGSKANKSKK
>NZ_CP029149.1|WP_120488474.1|627367_628306_+|ribose-phosphate-pyrophosphokinase
MAEQATYLFSTRTSKALAEKIAAHYGQELGKINFQEFSDGEFEPVLDQTVRGGRVFLIGSTFPPADNLMELLLMIDAAKRASAKNITVVIPYYGLARQDRKDKPRAPIGAKLVANLLTAAGATRIMTMDLHADQIQGFFEIPVDHLYASTIFVPYIQSLGLDNLTIASPDMGGAKRAKNYASHLGAEVVIAYKERKRANVVDDMFLIGDVKDRNVILIDDMIDTAGTLCKASDILIKNGAKSVRAIATHGVLSGKAYDNIQNSSMVEVIVTDSIPVQAEKSPKIKVLSCAPLFAEVMKSVHTYQSISSKFII
>NZ_CP029149.1|WP_160223928.1|624860_627221_-|tetratricopeptide-repeat-protein
MKKIIFPFFLLMLLVACKSTKKAQNKSVGLKGFYTYYNTLFNGKEAYEAEINNRKKNHQDNFYTDYISLLPNEEPELNSEKSNELGPENSVLFTNKNAIEPPQTGGSSLQVTEAKALKAISKYSVIKNGEERNKSLFDAYILLAKARLMMNKPVEALDALNTLVSNMPKYKKLSLAKIYQAEAYTRLGDYYKAEEVFQEAQKDPKIKKSYAKLLSLYYAEMLLKAGKKEKAVEELEEAFRLNKNRQLRSRIAYLRGQILNQLGKNDEARASFTTAYKYANSFEFEVKAQVEIAKTFTSGDNYDEAKKYVEDISKKGVYLSRRNEFYYALGLMADKAGKKDEADAYFRKSLEGEASDKQIRGLAFYQIGKAYFDKDDYIPAGAYYDSAIAVMTYAPQREKLAEQTKNIKKITQNYYLIKKNDSILALTKMSDAEREAYFGKIIQELKEKEEKEERERRRAERSEGFDTGDYNANSAFTSGRLEDFSSPRNKGGFYFANASTVSKGTNDFKQIWGNRTLADNWRYSNKMGSIEEEKQKAMGVESPKDPRRFEVAFYTEKIPTDEEQIAQLKKDRDTASLGLGRMYESYLSKTPLATKTLYDLVDSKPEDEVKLQALYTIFSINYEKTPEAAERAKQLIIQDFPHTPYAEFVKNPKNTNFSATSDPEVQKRYTEAYNLYSEEKFEESKNIIETTIENYPKDALIPKFELLRAFNTGKTVGKEVMILQLEQLALGYPKTMEGEKAKQMLKYLKSDVEVELRDEAGEKIDKAPEKKPAPKQQKPISEEDLE
>NZ_CP029149.1|WP_120488476.1|623304_624432_-|hypothetical-protein
MKQFFIFLTAMLLLVSCKKDKVDASSTMAFQESINDMASGLSTLEQIKFNEALYILKTFGVEGETDLERMKNLAHLLDAKNVNEILALADSIAIKNEIEWSSTAPPSLGETSIFNNDKASEYDPNDIKAAALELAVTEIKRDSVSGATGVKAVPRLVDNDGQPVEFSNAALEVTFEVYSGGEKLFSTKNLMQNNDFAGFNFNFIKLSADKVVDDKVDITVTVKTTHKKFKKSKRGIKVNPKSLNIPAPAVEEEPEETAPSTTDETPAETPEGDPKVTVSKFLSNLNAQNFRGAYSSSENPNWGSYDDFSNPVSGFGGVKSLSVKKLSPAKVEGSSASVSATYEVTDKEGNSTTLNVTFSLKNTNGEWKISNYKIN
>NZ_CP029149.1|WP_120488477.1|622717_623245_-|adenine-phosphoribosyltransferase
MKLIEKLNETIVNIPDFPKEGIQFKDITPIFLNPELYEEIIARFVENAKGKVDAVCGIESRGYLFGIAIAVALKVPFILIRKKGKLPPPFIGEKYDLEYGTSEIEMKTGHIKAGQRVLIHDDLLATGGTAIAAAKLVERQGAKATLFSFLIELEALGAREKIDKTGAELFSILKY
>NZ_CP029149.1|WP_160223927.1|621935_622631_-|tetratricopeptide-repeat-protein
MAKHKKQVEGKETVEFFQELDRETLKTEKFLERNSKLIIGIFIFILGGILGYFAYQQFVITPKNEEALKGYFAAQKNLELGKEADALGGKSAVNPGFLGTSKEFGDTKIGKLSAYNAASIKFKDGKYQEAYDLFNQFSSSNDILMALKYGAMADCKVNLNKNDEALSLFEKAISSSDDDYTAYYFTRKAGVLAISINKKAEAKKYFSTIDEKYQDYDNGMSDAYIEMVKYY
>NZ_CP029149.1|WP_120488479.1|621451_621934_-|6,7-dimethyl-8-ribityllumazine-synthase
MATVNLSEYKPLDITNADEFSIGIVVSEWNDFVTENLFKGCFETLIKEGVKEENISVIRVPGAFELSYASMQMCKSENYDAVVAIGCVIRGETSHFEFICSGVAHGITQCNTQTNTPAIFCVLTDDNSVQSIARSGGHLGNKGVEAAVTAIKMAYLRHHP
>NZ_CP029149.1|WP_120488480.1|620319_621081_+|succinate-dehydrogenase/fumarate-reductase-iron-sulfur-subunit
MSTHKGLNLTLKVWRQKNNKSKGQFETYKISGVSPDSSFLEMLDMLNENLVNEGKEPVAFDHDCREGICGMCSLYINGRAHGPDTGITTCQLHMRMFKDGETIHIEPWRSAAFPVIKDLVVDRSAFDRIMAAGGFISVNTSGNTLDANAIPVPKEDADKAMDAAACIGCGACVATCKNGSAALFVGAKVSQFALLPQGRVEAKRRVLNMVKAMDEEGFGNCSNTGACEVECPKGISLENIARLNREYLSAYVD
>NZ_CP029149.1|WP_120488481.1|618280_620293_+|fumarate-reductase/succinate-dehydrogenase-flavoprotein-subunit
MSVLNSKIPAGPLKDKWKNHKDHMNLVAPNNRDKIDVIVVGTGLAGGSAAATLAEQGYNVKAFCYQDSPRRAHSIAAQGGINAAKNYQGDGDSIYRLFYDTIKGGDYRAREANVYRLAEVSVNIIDQCVAQGVPFGREYGGQLDNRSFGGVQVKRTFYAKGQTGQQLLLGAYSAMSRQIGKGRIKMYNRHEMLDLVIVDGKARGIIARNLVTGEIERHSAHAVVIASGGYGNVYFLSTNAMGSNCSAAWKIHKKGAYFANPCFVQIHPTCIPVHGTQQSKLTLMSESLRNSGRIWVPKKIEDAVAVREGKLKPQDIKEEDRDYYLERRYPAFGNLVPRDVASRAAKERCDAGFGIENNDTKEGVFLDFSTEILKKGKEAALEKNIHNPTDQQIYDLGKAWVEEKYGNLFIMYEKITADNPYVTPMKIYPAVHYTMGGVWVDYNLMSTIPGCFVIGEANFSDHGANRLGASALMQGLADGYFVLPYTIADYLSADIRTGVIPTDTPEFEAAEKEVKDRINFFMTNKGTHSVDYFHKKLGNIMWNKVGMARNAKGLEEAIKEIEEVRNEFWKDVKVPGDANEMNIELEKALRVADFLELGQLMAIDALNRNESCGGHYREEYSTEEGEAKRDDEHYKYAAVWEYKGKDINSEVMHKEELIYENIEVKTRSYK
>NZ_CP029149.1|WP_160223931.1|633609_634497_-|tail-fiber-domain-containing-protein
MKNRLLFAVAVLGFGVQMKAQATDDYRGRVGINTKNPGATLHIESGNSDMKGIIIPRVSANEMKVMTAKPAFGEEQNALTIFLTEEMPIGDQNGKLKNVKEAGYYYYSHPAGLWQALGASTNGGGNSGGTFYAQDGTLTDDADHIRTVTLPSEMKHVLFTREAGNTSTEPVILVDGKVKTTAVNLNSDQRLKRDIQPIALDNKLSKLRPVTYYWNEKGKQKGGDNTLQYGFIAQEVERLYPEMVSTDSEGLKSVNYIQLIPVLTRALQEERARNDAQEKKIEELTKAVQTLKRNR
>NZ_CP029149.1|WP_160223932.1|634604_635390_-|hypothetical-protein
MKKTLYILAFVIGGIAYSQIKTNDVVSSNTITEQTAFLDASSSVAWNNSTNKGKGLVFPRTDLTTLAALVAFPNGLPTSYPTRLDGMIVYNTGTGETKTGAQKVKVTPGFYFYENKSTTLNGGTWKPLEGSKWTNDSANNRVKLTTLSDGTTAREDAKNLFVGDDGNLTVGAMKDASAKADRMVVADKEGKLKATVVPVKMQAATECKEETIGTINYGEFNKDGKQVSAFGFCMKRDNVFQWFYMYGGVGVTTGNATFGTF
>NZ_CP029149.1|WP_160223933.1|635404_636388_-|hypothetical-protein
MKQVIYRASVLCFIGFGALASAQVTTPYDGNVGINVENPEATLTVKSLQGRNNGTTRNLELNNGDGNNLMTVLNNGFVGLGTRQPSVKLHVEKGSVLVTEGNFTSRVDSNEGGRLYLDNPKKSTGKEVKTWAIFNMTNTATGAKYNPGLHFWAYAADGTNLNTQMIITDGGNVGIGSLYSNQKSPDEKLTVDGKIKTTSLAGTGDRPVYADANGVLKIGTGGGGAATPEVGFTRNIRTDSRSTVVMDQNEDGTATVDYFVRMTGIANNITFTPASASNKGRTVCFYNEKSGTGTITPQPIGPVQTVQPSQVACFISDGTVWLNSNGY
>NZ_CP029149.1|WP_160223934.1|636675_638178_-|glutamate--tRNA-ligase
MEKVRVRFAPSPTGALHLGGARTALYDYLFAKNQGGDFVLRIEDTDTARFVEGAEEYIMEALEWCGIIPDESPKHGGPYAPYRQSERRHIYDKYTQEILKTDYAYIAFDTAEELDKIRKEYEERGEVFAYNYQTRARLRNSISLPADEVERLLNENTPYVVRFKMPFDRVLNLEDIIRGKFSVNTNTLDDKVLVKNDGMPTYHFANIIDDHEMKISHIIRGEEWLPSMGLHILLYEAMGWEAPQFAHLSLILKPEGKGKLSKRDGAKFGFPVFPLDFYDKASGETFKGYREEGYFPEAFVNFLALLGWSPAEDREILSLDEMAKEFDLHKVHKAGARFSKEKAEWFNHQYLQKKSVAELVSLLKQIEGVAEANLSDEKLERIVCLMKERATFVKDIYNDGKFFFERPQSYDEKAVKKAWKEDTPAIMSGLVAVLENTDFKAEILKEAIHHYAEEKSLGMGRVMMPLRLCLVGELKGPDVPDILEILGKEESIKRLREVKL
>NZ_CP029149.1|WP_120488467.1|638298_640569_-|aconitate-hydratase
MIFDLDMIKKVYERYPERIAEARKVVGRPLTLSEKILYAHLWEGNATTAHQRGSSYVDFAPDRVAMQDATAQMALLQFMQAGKAKVAVPSTAHADHLIQAKENAEIDLKVGKSKNEEVFNFLGSVCDKYGIGFWKPGAGIIHQVVLENYAFPGGMMIGTDSHTVNAGGLGMVAIGVGGADAVDVMAGMPWELKMPKLIGVKLTGKMSGWTAPKDIILKVAGILTVKGGTGCIVEYFGEGAESLSATGKGTICNMGAEIGATTSTFAYDDSMRRYLAATGRQEVVDAADKVAEHLRSDAEVYAEPEKYYDQLIEINLSELTPHLNGPFTPDLATPVSEFREKAEANGWPLDVEWALIGSCTNSSYEDLSRAASIVEDAVAKGVKPKAILGINPGSEQVKFTAERDGFLNSFRKFDNARIFTNACGPCIGQWDREGAEKQEKNSIIHSFNRNFAKRADGNPNTHAFVASPEMVAAVAISGRLDFNPITDTLTNEAGEQVKLAEPKGYELPTKGFAVDDNGYQAPSEDGSNVQVIVSPTSDRLQLLEAFPAWDGKNIEGAKVLIKAFGKCTTDHISMAGPWLKYRGHLDNISNNMLIGAVNAYNMETNNVKNQLTGEYGEVPAVQRQYKAAGIPTIVVGDENYGEGSSREHAAMEPRHLGVRAVLVKSFARIHETNLKKQGMLGLTFNDKADYDKIQEDDTVNFLDLDQFAVGKPLTLEFVHKDGSKDIIIANHTYNEQQIDWFKAGSALNLIKQQNNK
>NZ_CP029149.1|WP_160223935.1|640853_641975_-|3,4-dihydroxy-2-butanone-4-phosphate-synthase
MSEIILNTIPEAIEDLKNGKVIIVVDDEDRENEGDFLSAAELVSPEVINFMTIHGRGLICTPLPEKRCDELGLDIMVYRSSDPKETAFTVSVDLLGKGVSTGISASDRAKTIAALMDENSKPTDFMRPGHIFPLRAKSGGVLKRAGHTEAAIDLTRLAGLKEGGVICEIMNEDGTMARLPQLIELAKKLNLKIISIEDLIDYQLKKGDLVNKIEERPVKTFYGDYDFHVFQEKHTDQLHFALTKGSWEFDEPVLVRVQSSSVYFDVLHQLTNGEKPLLDRITKLINDEGKGALVFINNVSNAENTLRKLQQFNSQQDGQKPITNPNFAEYGIGTQILKKLGISKFRVISQNPEHKPMISGYGVEVTEMVKLGA
>NZ_CP029149.1|WP_120488465.1|642116_642392_-|hypothetical-protein
MVLSAFWPFYQYLWTVYFFIMFIIGFWCIFMFATVVVPFWLTAGLKEYFGKVKPFDPEQVRRKRLNEQEGVEVIYSQPKGDGPFIHHGHHH
>NZ_CP029149.1|WP_120488464.1|642620_644015_+|class-II-fumarate-hydratase
MDYRIEHDTMGEVKVPADKFWGAQTERSRNNFKIGEEGSMPKEIIEAFAILKKAAAFANNELGVLPTEKRDAIATVCDEILAGKLNDQFPLVIWQTGSGTQSNMNLNEVISNRALVNNGGKLGEKSFIHPNDDVNKSQSSNDTYPTAMHIAAYKKVVETTLPALEKLRNTLDEKAKAFQNVVKIGRTHLMDATPLTLGQEFSGYVAQLDYARKAIINTLEHLKELALGGTAVGTGLNTPKGYDTKVADYIAKFSGHPFVTAPNKFEALAAHDGIVETHGALKQLAVSLYKIAQDIRLLASGPRSGIGEIFIPENEPGSSIMPGKVNPTQNEALTMVCAQVLGNDTTISFAGTQGNYELNVFKPVMAFNFLQSAQLLADAMHSFNDHCAVGIEPNHTRIKELLDKSLMLVTALNTHIGYENAAKIAKTAHKNGTTLKEEAINLGLLTAEQFDEWVKPEDMVGSLK
>NZ_CP029149.1|WP_160223936.1|644166_646935_-|propanediol-utilization-protein
MKKIFILITAALGAFGYSQNYWQKISTKAGKNNEVEQFYKLNLHQLRKDLNTQLSAKNAEMIIEIPNVEGKLEKFKVRSFPVVDEAMAAKYQLGSYQGVSLENSRRTIRFSVSPYDFQSMLSTDEGYSFIDPERKQKDVYRVHPKSLKAKGRAFECTTSEPKSDIQGLDHLYKNAEAYKKNTLFNISSSDRKYRTIRMAISVTGEYTQVFGSVEKALAQINATLTRVNQVYERDLALHLNLVNTPELIYTDPNTDPYSDADLGVAGEWNVELQRNLTKVLGNDAYDLGHLFGASGGGGNAGCIGCVCIDPEPDPFGDSMDTQKGSAFTSPSIDDEPFGDAFDIDYVAHEIGHQLGANHTFSHDIERSDVQVEPGSGSTIMGYAGITEANVQQSTDPYFNYVSLNQIREVLSKATCAQKTSIQNTLPVISPLKSYTIPKKTPFVLSAQVTDKENDPLTYTWEQQNSAETKLVKISGDRKDGANFRSLKPGTEPIRYFPKLENVIAGKLISEDDWEAVSNIVKEMKFVLTVRDNHPTLNQQQVASAEQNISVGKEGPFAVTSGILHYGVSKPILWDTANTQNAPYSVANVKIDYTQDEGKNWTILSESTPNDGNEKLNFPASLAGKKIQIRISAIDNVFYTVSKPLLVTKLEGCSSQAPDHFTVENERRKALLSWEGAENATYSIRYKKKTDTGWKSFTSESPSAEISVGVHHLDFGVDYEVQVANICSGTVGNYTQSQTLHFPALEYCGLKANSSEFEYISRVKVTDAGGKLILDNKSAGDGYKDYVTDSSKVITLKQGSKGNKLSITVVYPSDEDFYETLSVWIDFNGDAKMSEAERVVKHFIPDPSNGNKGSIVAHFNIDVPDDAIIDTQEYYRMRIALKVGPSINSAPASSCNGRLTGSRVVVDNYGYGEVEDYRIKIIK
>NZ_CP029149.1|WP_160223937.1|646939_647785_-|T9SS-type-A-sorting-domain-containing-protein
MIRNLCLAFALLSGLSKAQDVIFSERFDTDDPNHYNDWVILDDDRDGETWKLSLGSDFAESAGWDNTNSFMMVATSYISRPIPGPLDADDVLISPEITIPATGKTELSYKIGVVLDERNGFKLNDIDYWLFILADGQKYFPTLTPTDHTNFSSANSAQERKFDISAYKGKKIRLCFRHRAFAQFQLLLDNIKITHQPDLSVSDTPNKEEIIYSVYPNPAYDVLHLQGFDSSSSYIIYDASGKAVNKGNGEEDINLRALPAGAYIIKVKNNEVEKTFKFIKK

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Crispr_ID: NZ_CP029149_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP029149_4

913907-914060

Orphan

Consensus_repeat	Method
CCCACTAGCGTGGGGAGCAATTATTT	CRISPRCasFinder

2 spacers

The CRISPR arrays of NZ_CP029149_4

>merge|NZ_CP029149|4|913907-914060|CRISPRCasFinder
CCCACTAGCGTGGGGAGCAATTATTTCATTTTCCTTTCCGACAGGCCCATTTTTATTCCCGACAAGTTCATTTTTGTTCCCGACAGCCCACTGGCGTGGGGAGCAATTATTTTTTAAGTGCTCCACCTGCAAGGTGCGTGGAGAGGAATTGTTT

>NZ_CP029149|4|3|913907-914060|CRISPRCasFinder
CCCACTAGCGTGGGGAGCAATTATTT	CATTTTCCTTTCCGACAGGCCCATTTTTATTCCCGACAAGTTCATTTTTGTTCCCGACAG
CCCACTGGCGTGGGGAGCAATTATTT	TTTAAGTGCTCCACCT
GCAAGGTGCGTGGAGAGGAATTGTTT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP029149.1\|WP_120488236.1\|900103_900817_-\|biotin--[acetyl-CoA-carboxylase]-ligase	unknown	unknown	gnl\|CDD\|319741
NZ_CP029149.1\|WP_160224061.1\|905787_910167_+\|S8-family-serine-peptidase	unknown	unknown	gnl\|CDD\|173791
NZ_CP029149.1\|WP_120488226.1\|916420_916834_+\|DUF2147-domain-containing-protein	unknown	unknown	gnl\|CDD\|378304
NZ_CP029149.1\|WP_120488222.1\|920876_921296_+\|SufE-family-protein	unknown	unknown	gnl\|CDD\|376883
NZ_CP029149.1\|WP_120488233.1\|904011_904875_+\|phosphatidate-cytidylyltransferase	unknown	unknown	gnl\|CDD\|366491
NZ_CP029149.1\|WP_160224066.1\|923718_924399_-\|MotA/TolQ/ExbB-proton-channel-family-protein	unknown	unknown	gnl\|CDD\|223881
NZ_CP029149.1\|WP_120488229.1\|912608_913814_+\|acetate-kinase	unknown	unknown	gnl\|CDD\|234680
NZ_CP029149.1\|WP_160224060.1\|901300_903268_+\|ATP-dependent-zinc-metalloprotease-FtsH	unknown	unknown	gnl\|CDD\|273520
NZ_CP029149.1\|WP_160224064.1\|917989_920488_-\|ATP-dependent-Clp-protease-ATP-binding-subunit	unknown	unknown	gnl\|CDD\|223616
NZ_CP029149.1\|WP_160224063.1\|914132_916286_-\|ribonuclease-R	unknown	unknown	gnl\|CDD\|273947
NZ_CP029149.1\|WP_120488235.1\|900906_901275_+\|ribosome-silencing-factor	unknown	unknown	gnl\|CDD\|376779
NZ_CP029149.1\|WP_120488223.1\|920629_920875_+\|uroporphyrinogen-decarboxylase	unknown	unknown	unknown
NZ_CP029149.1\|WP_120488220.1\|923315_923714_-\|biopolymer-transporter-ExbD	unknown	unknown	gnl\|CDD\|223917
NZ_CP029149.1\|WP_120488232.1\|904881_905538_+\|phosphatidylserine-decarboxylase-family-protein	unknown	unknown	gnl\|CDD\|235400
NZ_CP029149.1\|WP_120488225.1\|917500_917893_+\|DUF3127-domain-containing-protein	unknown	unknown	gnl\|CDD\|378639
NZ_CP029149.1\|WP_120489650.1\|921295_922273_+\|glycosyltransferase-family-9-protein	unknown	unknown	gnl\|CDD\|340821
NZ_CP029149.1\|WP_160224062.1\|910482_912561_+\|phosphate-acetyltransferase	unknown	unknown	gnl\|CDD\|235537
NZ_CP029149.1\|WP_120489651.1\|903517_904000_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|376839
NZ_CP029149.1\|WP_160224065.1\|922414_923278_-\|ferric-siderophore-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|236768
NZ_CP029149.1\|WP_160224059.1\|895335_899709_-\|S8-family-serine-peptidase	unknown	unknown	gnl\|CDD\|173791

Protein	Function_ID	Function_description	E-value
NZ_CP029149.1\|WP_120488236.1\|900103_900817_-\|biotin--[acetyl-CoA-carboxylase]-ligase	gnl\|CDD\|319741	cd16442, BPL, biotin protein ligase. Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an activated form of biotin, biotinyl-5'-AMP, from substrates biotin and ATP followed by biotinylation of the biotin carboxyl carrier protein subunit of acetyl-CoA carboxylase. Biotin protein ligase (BPL) is the enzyme responsible for attaching biotin to a specific lysine at the active site of biotin enzymes. Biotin attachment is a two step reaction that results in the formation of an amide linkage between the carboxyl group of biotin and the epsilon-amino group of the modified lysine.	1.52954e-31
NZ_CP029149.1\|WP_160224061.1\|905787_910167_+\|S8-family-serine-peptidase	gnl\|CDD\|173791	cd04842, Peptidases_S8_Kp43_protease, Peptidase S8 family domain in Kp43 proteases. Kp43 proteases are members of the peptidase S8 or Subtilase clan of proteases. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). Kp43 is topologically similar to kexin and furin both of which are proprotein convertases, but differ in amino acids sequence and the position of its C-terminal barrel. Kp43 has 3 Ca2+ binding sites that differ from the corresponding sites in the other known subtilisin-like proteases. KP-43 protease is known to be an oxidation-resistant protease when compared with the other subtilisin-like proteases.	1.36411e-45
NZ_CP029149.1\|WP_120488226.1\|916420_916834_+\|DUF2147-domain-containing-protein	gnl\|CDD\|378304	pfam09917, DUF2147, Uncharacterized protein conserved in bacteria (DUF2147). This domain, found in various hypothetical prokaryotic proteins, has no known function.	3.90826e-27
NZ_CP029149.1\|WP_120488222.1\|920876_921296_+\|SufE-family-protein	gnl\|CDD\|376883	pfam02657, SufE, Fe-S metabolism associated domain. This family consists of the SufE-related proteins. These have been implicated in Fe-S metabolism and export).	2.6055e-63
NZ_CP029149.1\|WP_120488233.1\|904011_904875_+\|phosphatidate-cytidylyltransferase	gnl\|CDD\|366491	pfam01148, CTP_transf_1, Cytidylyltransferase family. The members of this family are integral membrane protein cytidylyltransferases. The family includes phosphatidate cytidylyltransferase EC:2.7.7.41 as well as Sec59 from yeast. Sec59 is a dolichol kinase EC:2.7.1.108.	3.61574e-44
NZ_CP029149.1\|WP_120488229.1\|912608_913814_+\|acetate-kinase	gnl\|CDD\|234680	PRK00180, PRK00180, acetate kinase A/propionate kinase 2; Reviewed.	0
NZ_CP029149.1\|WP_160224060.1\|901300_903268_+\|ATP-dependent-zinc-metalloprotease-FtsH	gnl\|CDD\|273520	TIGR01241, ATP-dependent_zinc_metalloprotease_FtsH, ATP-dependent metalloprotease FtsH. HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH. [Cellular processes, Cell division, Protein fate, Degradation of proteins, peptides, and glycopeptides].	0
NZ_CP029149.1\|WP_160224064.1\|917989_920488_-\|ATP-dependent-Clp-protease-ATP-binding-subunit	gnl\|CDD\|223616	COG0542, clpA, ATP-binding subunits of Clp protease and DnaK/DnaJ chaperones [Posttranslational modification, protein turnover, chaperones].	0
NZ_CP029149.1\|WP_160224063.1\|914132_916286_-\|ribonuclease-R	gnl\|CDD\|273947	TIGR02063, Ribonuclease_R, ribonuclease R. This family consists of an exoribonuclease, ribonuclease R, also called VacB. It is one of the eight exoribonucleases reported in E. coli and is broadly distributed throughout the bacteria. In E. coli, double mutants of this protein and polynucleotide phosphorylase are not viable. Scoring between trusted and noise cutoffs to the model are shorter, divergent forms from the Chlamydiae, and divergent forms from the Campylobacterales (including Helicobacter pylori) and Leptospira interrogans. [Transcription, Degradation of RNA].	0
NZ_CP029149.1\|WP_120488235.1\|900906_901275_+\|ribosome-silencing-factor	gnl\|CDD\|376779	pfam02410, RsfS, Ribosomal silencing factor during starvation. This family is expressed by almost all bacterial and eukaryotic genomes but not by archaea. Its function is to down-regulate protein synthesis under conditions of nutrient shortage, and it does this by binding to protein L14 of the large ribosomal subunit, thus acting as a ribosomal silencing factor (RsfS) by blocking the joining of the ribosomal subunits. This family is structurally homologous to nucleotidyltransferases.	5.45744e-39
NZ_CP029149.1\|WP_160224066.1\|923718_924399_-\|MotA/TolQ/ExbB-proton-channel-family-protein	gnl\|CDD\|223881	COG0811, TolQ, Biopolymer transport proteins [Intracellular trafficking and secretion].	5.51991e-35
NZ_CP029149.1\|WP_120488220.1\|923315_923714_-\|biopolymer-transporter-ExbD	gnl\|CDD\|223917	COG0848, ExbD, Biopolymer transport protein [Intracellular trafficking and secretion].	3.43726e-26
NZ_CP029149.1\|WP_120488232.1\|904881_905538_+\|phosphatidylserine-decarboxylase-family-protein	gnl\|CDD\|235400	PRK05305, PRK05305, phosphatidylserine decarboxylase family protein.	2.58218e-90
NZ_CP029149.1\|WP_120488225.1\|917500_917893_+\|DUF3127-domain-containing-protein	gnl\|CDD\|378639	pfam11325, DUF3127, Domain of unknown function (DUF3127). This bacterial family of proteins has no known function. However, it does show distant similarity to pfam00436, with proteins such as Prevotella buccalis HMPREF0650_0099 being similar to both families. This suggests that this family may have a DNA-binding function.	8.05063e-32
NZ_CP029149.1\|WP_120489650.1\|921295_922273_+\|glycosyltransferase-family-9-protein	gnl\|CDD\|340821	cd03789, GT9_LPS_heptosyltransferase, lipopolysaccharide heptosyltransferase and similar proteins. Lipopolysaccharide heptosyltransferase (2.4.99.B6) is involved in the biosynthesis of lipooligosaccharide (LOS). Lipopolysaccharide (LPS) is a major component of the outer membrane of gram-negative bacteria. LPS heptosyltransferase transfers heptose molecules from ADP-heptose to 3-deoxy-D-manno-octulosonic acid (KDO), a part of the inner core component of LPS. This family also contains lipopolysaccharide 1,2-N-acetylglucosaminetransferase EC 2.4.1.56 and belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.	9.53299e-39
NZ_CP029149.1\|WP_160224062.1\|910482_912561_+\|phosphate-acetyltransferase	gnl\|CDD\|235537	PRK05632, PRK05632, phosphate acetyltransferase; Reviewed.	0
NZ_CP029149.1\|WP_120489651.1\|903517_904000_+\|hypothetical-protein	gnl\|CDD\|376839	pfam02589, LUD_dom, LUD domain. This entry represents a domain found in lactate utilization proteins B (LutB) and C (LutC), as well as several uncharacterized proteins. LutB and LutC are encoded by th conserved LutABC operon in bacteria. They are involved in lactate utilization and is implicated in the oxidative conversion of L-lactate into pyruvate.	5.88209e-05
NZ_CP029149.1\|WP_160224065.1\|922414_923278_-\|ferric-siderophore-ABC-transporter-substrate-binding-protein	gnl\|CDD\|236768	PRK10819, PRK10819, transport protein TonB; Provisional.	6.72998e-06
NZ_CP029149.1\|WP_160224059.1\|895335_899709_-\|S8-family-serine-peptidase	gnl\|CDD\|173791	cd04842, Peptidases_S8_Kp43_protease, Peptidase S8 family domain in Kp43 proteases. Kp43 proteases are members of the peptidase S8 or Subtilase clan of proteases. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). Kp43 is topologically similar to kexin and furin both of which are proprotein convertases, but differ in amino acids sequence and the position of its C-terminal barrel. Kp43 has 3 Ca2+ binding sites that differ from the corresponding sites in the other known subtilisin-like proteases. KP-43 protease is known to be an oxidation-resistant protease when compared with the other subtilisin-like proteases.	1.89731e-45

>NZ_CP029149.1|WP_120488229.1|912608_913814_+|acetate-kinase
MEILIINSGSSSLKYQLIDSQTGESKARGLVDRIGIDGSTIKYVALKNGKEIEVKKQLPIANHEEGLNLVTELLCDAEVGVISNPDDIKGVGHRVVHGGERLVQPTIITDEIEKIIEELIPLAPLHNPGNLSGIRVARKLFAKATHCAVLDTAFHQTMPAKAYRYAIPAEFYEKNGVRAYGFHGISHKFVDGEARKLLNKPNAKNITIHIGNGASMSAVNAEGKCVDTSMGFTPLDGLVMGTRCGQIDPGVIFYMGSQLGLSNDEINTILNKKSGMLGVSGYSDARDVSDKYHTGDANAILCYEMYAYRIKKFIGAYTAALNGLDSIIFTAGLGENDALVRKLVCQDLSFLGIELDEEKNEQLNHPKHPVEVQKDGARVKIFIIPTNEELQIVNEIIDLVK
>NZ_CP029149.1|WP_160224062.1|910482_912561_+|phosphate-acetyltransferase
MNKSIYIITPDSYSGKILVSLGIMQTIIRNTPNVAYFKPILERADDNHISTMISQFNLNMKYEEAFAFTRDQAITLKNQGKISEVYDTIINKYKALEERFDFVLVEGVDLAKESSTFDFNFDISIIRSLNTPALAVVKDSFTTEEALLSHTRVELNTLLENEIKVLGLFINKAENHTSETKQTLEREFKNIHFTIIPQEEILEKPTLKEIANALNADFLYEDKNVNVIAQKTIVGGMRLHNFLPRLTENCIAVIPADRSDLIVGTLAASFSTNYPRVAGIVLYGGFEPEEAISKIIEGTSIGVPIIHAQTGTYETANIIGNIRSRIYPESEEKIKLCLQLFDKHTDISDLNTRISSFKSDTLTPRMFQYNMVKAAKKAQKHIVLPEGTDDRILTAASQLASDELATLTILGERDGILRRVNELGLKWNNDRISIINPIESPKYKDYYEKLYELRKAKGLELSQAKDLMLDVSYFGTMMVFLGDADGMVSGAVNTTAHTILPSLQFVKTKAGVNTVSSVFFMLLPDRVLVYGDCAIVPNPTAEQLAEIAITSADSAKAFGIEPKVALLSYSSGNSGSGADVDKVRSATAIVKEQRPDLLVEGPIQYDAAVDPKVGSQKIPNSPVAGQANVLIFPDLNTGNNTYKAVQRETGALAIGPMLQGLKKPVNDLSRGATIPDIYNTVLITAIQAVMED
>NZ_CP029149.1|WP_160224061.1|905787_910167_+|S8-family-serine-peptidase
MTKSIFKVGVLARNLPIALCYLFASAVFAQNAEEIRAIQGKTDLKALSQLSSRIQKEEMSTARLQSKAKELNIPFTGEVDGKLYQLQGFNHNGLPFYYITDNVGAAESVYTSILQNSPAFNLQGDGITLREWDAGAVRISHQEFGGRAKMGDSSKFPNSHSTHVAGTMIASGIDKQAKGMAPKAELIAYDWTDDSKEMSDAATNGALLSNHSYGTTAGYQQGNWSGFTGWHWFGEEDETEFIGYGHYGEKDAKWDLISRNAPYYLFLKAAGNPRGGGPEPGGVHYVRRKENQRIVWVRSTKTRQKNGGASGFDCIANGGTSKNGLIIAAAHKIPGGYKQPSDVKVASFSAFGPTDDGRIKPDLAGIGVGVYSTNSTGDDQYTSLNGTSMASPNVTGSLALLQEHHNKLYRSFMKSATLKALAIHTANEAGKHPGPDYQFGWGLLNAYKAAKVLSTKDKYSKVEEATLNNNTPYTVKLTALGNTPLIVTIVWDDAVVEKLPDYVLNNRESVLVNDLDLRISDGATTFFPWVLDVENPANAATKGNNVKDNVEQVVIENPVAGQEYTITVSHKGSLRKNDNDGKLVPATSQDFSLIATGINTGVANDLALKSVSLPQAKDYTDQTPVTVEVENLGSTSATGAKLKYKLVNADTDTVEHTGEVALEEIAKGVTLSKSFNVDLSKSFVNYSIEAEVEFTGDEVAINNAVSAKAYGIIATVENVGESYSYGFEEELEKSGWTVEDTDGNGRTWRVYPDIKLARTGKSFGVNFPNSTKGADDWLFSNPIKVKGGKPYRLRFYLRKLNKDAEESLKVFYGAQPDKTSMTNQLGEKLIASEDLEYQQVIREFTPTQDGIIYFGFHNKVDADKSSYAIGIDDILVRRSEGKPDADFKPSKTKANSYETIELLNQTANAPSQPATYEWSFSPNTIEYKDGTASTSEHPKVRFIEEKAYSVTLKAKNTSGEDSIQKTALITIKNTPTKAVFTPSNSRAYAGEGIVLINQSTGDPLPTEFEWTVSPSEDAEFINGTSTTSSSPILKFNKEGDYTISLKATSPHNANTVKQKISISKVLNKVTHLTATQRNNTVDLKWVRPLIAPIYTEGFELDMPADITVIDANRDGNSWEITTKYPNSGQKGVANFSSGKTGDITVDDWLITPKIKSGAEVLKYYEKHFFKERYDVYVVPAPTSGNAPTIDEIKNTGSIVYKFDAGYTSGDFKQNTVDIKQHTAQDFFVAFHHRTQKEDKGFYFALDDIQVGYRDRVSADKTPLANKKQSASVPISDLKNNANEDILILDTKPDELLTVNSQGLPTEMGVLNLPTLKGYEIVRNNVKLTDITDINTLKHTDTLTQTGSYTYDVYAVYSDGKKSDKVSVSITISDLSSSEVVKGGLKIYPNPSDGRFIIELGSGTSSLEAQVYDLSGKLIFKKEYSGSRADLNLTQYPKGVYLLHLTNNKGEKQTAKLIVQ
>NZ_CP029149.1|WP_120488232.1|904881_905538_+|phosphatidylserine-decarboxylase-family-protein
MKLHREGKGSIVLATVIVLAVYILSTLFLSAWAWLITLPFLVLYALVLWFFRVPNRQIGEYKTEVIAPVDGKVVMIKEVEETEFLKEKCIQVSIFMSPLNVHICRYPVTGKVIYKKYHKGKYLMAWNEKSSTDNERTTVAVETQTHHKIVFRQIAGYIARRIVFYTNVGDDAKAGHEFGFIKFGSRMDVFLPLDTQILCKIGDTTKGGLDTIAQLKDH
>NZ_CP029149.1|WP_120488233.1|904011_904875_+|phosphatidate-cytidylyltransferase
MDKNFFQRIVFGLLYCLVVVFCTHPMGSELLQNIFPVQQYQLYYGLIVFFILVGLWECVRIMEFRKGWERLAVFPIAILILYRFSKKYFYHGFSFEFNLSEILGLSLILIAVITLFRFKSELDFESGKLIFTLIYVPLTFGYALALPYYNSENTFSLEPLFLFILIWSSDSFAYLSGRLFGKHKMAPTISPKKTWEGFAGGVLLTLIFSYFIEQKFGYLRGNWMVVGFLVAVFAPMGDLVESQLKRTFNVKDSGNIIPGHGGILDRLDSFMICAPVLYLYFILDKLL
>NZ_CP029149.1|WP_120489651.1|903517_904000_+|hypothetical-protein
MDYKFAQLFSHSGGIFSYCVDEAEALGILNQIIKNEDLKSVFCCDEDLKNFLSVLNVPQSTELTLNNDAALITCEYLIAHNGSIMLSYNNILHYHSSRLPKKVIIMANVSQIVPDLNMAMMKIKRRKTMLKNLTSISGSQSKLGGTEANHTKLFLLLLED
>NZ_CP029149.1|WP_160224060.1|901300_903268_+|ATP-dependent-zinc-metalloprotease-FtsH
MNSKGFNWFFPIVIIGILYIFFQPSFGGADAKRIDEDTFFQKLKEGKVSKVVVYKDTDKAEVFLTKEAKTEHINNKPSMNPLDGLTTRVVPDYDFTFGDIKSFQDEFKKVKASNPEVQTKMDFSKERNPLVEILLPILMWVGLLGIFYYFIFRRMNGGSGGGMFSIGKSRAKLFDEKDKMQITFKDVAGLEGAKEEVQEVVDFLKNADKYTKLGGKIPKGMLLVGPPGTGKTLLAKAVAGEAQVPFFSLSGSDFVEMFVGVGASRVRDLFAQAKAKSPAIIFIDEIDAIGRARGGKNFTGGNDERENTLNQLLTEMDGFGTDTNVIVMAATNRADILDKALLRAGRFDRSIYVDLPELHERREIFEVHLKNIKIDDSVDREFLAKQTPGFSGADIANVCNEAALIAARNGRESVTKQDFLDAVDRIIGGLEKKNKAIKLSEKKRVAYHEAGHATVSWLLEHAAPLLKVTIVPRGRSLGAAWYLPEERQLTTTEQMLDEMCATLGGRAAEQVIFNNISTGALSDLERVTKQAQAMVTIYGLSENIGNISYYDSSGQSDYSFNRPYSEETATKIDAEIKFIIENQYQRAISILTDNKDKLDILANKLLEKEVIFREDLEEIFGKRAWDPELTEQPLQEELNKEQDSTQEAEEIKLEN
>NZ_CP029149.1|WP_120488235.1|900906_901275_+|ribosome-silencing-factor
MNKLTEKQLLIDKIVEAIQDTKGEDIKIFDLSTIENSVTETFIICSGNSNTQVSAIAGSIEKKVRNELKDRPWHVEGADNALWILVDYVSVVVHIFQKHIRDYYEIEELWGDAKITEIQNLD
>NZ_CP029149.1|WP_120488236.1|900103_900817_-|biotin--[acetyl-CoA-carboxylase]-ligase
MYPLFYLSESLESTNEAILNYHTPSRPNIAIYTFNQINGKGQYGNTWKMPKDQNIAYSLLIDASLIPIGGNFVNFYTAVIIRDFLDNLSDEEVFIKWPNDIIINRKKVVGILIEQIKIDGKSFYIIGIGINVLQRDFSELTKAGSILTQTHQRFNLTSLSENFHFYFTKHITHQPSYNILERYNHHLFCRNSVALFSKSNIRQNGIIQYADEKGFLHILLEKDGLQKFFHKEIEMLY
>NZ_CP029149.1|WP_160224059.1|895335_899709_-|S8-family-serine-peptidase
MRKSTLEFGSFTRKLPVALCYLFATAVFAQNAQEVKVLQSKTNLKGLNLLGKQFRKGTLSRAQLESRAKEMNIPFTTEFGGKFYQLQGFNAKGFPLYYVTSNAGAAEGTGVSRLQTSPGLELQGEGIVLREWDGGAVRLTHQEFGGRAKMGDTSTRLNSHSTHVAGTMVASGVDKKAKGMAPKAELIAYDWNDDEDEMTTAATNGALLSNHSYGYLGGFEYGNWSGATGWHWLGTDDDTEYVGYGHYGETDAQWDLISKNAPYYLAVKAAGNPRGDGPEPGGAHYVRKLENGKLVWAKSTKVRQKNGGANGFDCINHGATGKNGLIIGAAHKIPGGYKQPSDVKAASFSAFGPTDDGRIKPDLAGIGVGVYSTTSTGDSQYTSLSGTSMASPNVTGSLALLQEHHNKLYSSFMKSATLKALAIHTANEAGEHPGPDYQFGWGLLNTFKAAEVLSTKNKYSKVEEVTLNNNGTYTLKLTATGSAPLVVTIVWDDAVVEKLPDATLNNRESVLVNDLDLRVSDGATTFFPWKLDVNNPANAATKGDNTKDNVEQVVIENPVAGKEYTITVSHKGDLKKNDDQGKLVPAASQDFSLIATGINNGVSKDLALKSVSLPPAKEYTNQTPVTVEVENLGSASATGAKLKYKLVNVDNGNAVEHTGEVALEEVAQGKTLSKSFNVDLSKSFVNYNVEVEVVFVGDEVTMNNTASVSAYGVVASVENPGESHFFGFEEDFEKSGWVSKDVDGNGRTWMKYTDADLANTGKSFAVNFPNRAKGTDDWLFSNPIKVKAGKLYMLELYAGRFQNDEENLEFFYGDSPEVSAMTNKLGDKLTLAPSYNKVNREFTPTKDGVIYLGFHNKMDADKASYAVAVDDVLVRFAEGKPSADFTVAKPRVNSYETVQLNNNTTTASTQPATYEWSFSPNTVEYKDGTTSTSKDPKVRFTEEKQYSVTLKATNSSGNDVKEKKDFITVKNTPSQAKFITSGNSIFETETVAFTNKSTGDPLPTSFEWTVTPSDNTEFVSGTTSTSNNPVVKFNKSGDYKVSLKATSPQNETTAEVDIKVAGVHNSVKDLSATQENNKVNLKWVRPNMNPSYTEGFESGKIPTEMTVYDNNADKMSWMISAFNKASGNYGLLNYGWYFRSMDVDDWIVTPKIKGGAEVLKYFVKHDYVERYDVYVVKAPASGKAPTIDEIKATGEIVYKFDGTEKTKGTFVEREVDIKEHSKDDFFVVFHHRTTKDDDALLLALDDIQIGYKDNVSSDKTVAAKPSDEASVDLKQVVREGTKILKSGDFEDPYKAEAREQVPVEFGATDLPKLEKYEIVRNNVKLTDINDYNTLKHTDNLTQTGTYTYDVYAVYSDGKKSDKASVTIVVDNLSASEVVKGGLKIYPNPSNGRFTIELGSGTSSVQAQVYDLSGKLLFKKDYSGSRADLDLTHYPKGAYLLHLTNSKGEKQTAKLIVQ
>NZ_CP029149.1|WP_160224063.1|914132_916286_-|ribonuclease-R
MAKKRKYRSKKNDNKLKEIGRQIMRFLNQNTSKTYNYKQISDAIEHKNPRQREQVIQALHLLRAQEKIKETEKGRYAANILIEATVEGIIDFNQSGNAYVNAEGIDEDIFIHSKNVKDALQGDKVLVVTYHYKGKRLEGSVLQVLERKKDSFVGTFEFIKHKEFGFVVGDKKTINTDIFIAKSHFNGAQNGDKVVVRILKWEPQSKNPEGEIIRILGKPGEHETEIHSILADYGLPHDFPEEVEQEAAHIDRSIKEEEVQKRRDMREVLTFTIDPKDAKDFDDALSLQKLENGNWEVGVHIADVSHYVVPDSLLDEEAYHRATSVYLVDRVVPMLPEILSNDLCSLRPNEDKYTFSAVFELNDNAEIQKQWFGRTLIHSRRRFTYEEAQERIETQEGDLAEEILTLDRLAKILREKRIKDGAITFDRSEVRFNLDENNEPIGVYFKMSKDANHLIEEFMLLANKKVSEFISLNQRKEPTHKTFIYRIHDNPDPTKLEALRDFVSTFGYKMDISNPKNIAQSMNHLLKEVKGKGEENMIETLAMRSMSKAKYSTEPIGHYGLGFDYYTHFTSPIRRYPDIIAHRLLQYYLDKGKSVDASELESQCKHCSDMEMLASNAERESIKFMQVKFMEKHIGEVFTGIVSGVAEFGFWVEIPENGAEGLIKLRDLMDDSYTYDPQTHSVIGSRTGNEYRLGDPVQIKVMKANLLQKQLDFKIIS
>NZ_CP029149.1|WP_120488226.1|916420_916834_+|DUF2147-domain-containing-protein
MKKLIFATALVLGSLASAQIEGKWKTIDDETGKAKSVVEIFKKSDGKYYGKILQLMKPPKNENCVKCKDDRKDKPLIGLEIIRGLKKDGDEYSGGTITNPADGRDYKTIIIKDGNTLKVKALLLGIAVRTQVWHAVK
>NZ_CP029149.1|WP_120488225.1|917500_917893_+|DUF3127-domain-containing-protein
MELQGTIKKIFEIQSFPSGFQKREMILLTQEQYPQPVSIEFLSEKMNLLDNVSEGDNVKVGINIRGREWVNPQGETKYFNSITAWRLEKVADNGGYSEPTQATPAPEQEVQDTSSSTNVFEEDEDDDLPF
>NZ_CP029149.1|WP_160224064.1|917989_920488_-|ATP-dependent-Clp-protease-ATP-binding-subunit
MDYKLSEDFKKVLSQSTNEARRLNSEFVNTEHLLLGIVKTENTARDLLQSLNADLTQIRRKIENLSEAVAPSPLSEPKQSIPLTKMANSAILRAQLECRLYQSEEVSAIHLLLGILHKQEDPAAHILAAYDIDYNRVEEELKSTLKDSDATQPKMGAYEDEDDREEYNQMKHLTGSISSGKTKTPTLDNFGRDLTALARDGKLDPVIGREKEIERVSQILSRRKKNNPLLIGEPGVGKSAIAEGLALRIHQKKVSRVLYNKRVITLDLASLVAGTKYRGQFEERMKAIMTELEKNRDVILFIDELHTIVGAGGAAGSLDASNMFKPALARGEIQCIGATTLDEYRQYIEKDGALERRFQKVMVEPTSVEETIQILNQIKDKYEEHHNVTYTSEAIMACVNLTSRYITDRFLPDKAIDAMDEAGSRVYIKNIKVPTKIIELEQKIEEVKSLKQKAAKAQDYLEARTYKEEEEHLLRELQVVQDEWDKNTKEAKELVTEENVAEVVSMMSGIPVTKVGKNELDKLAQMNELINGKVIGQTDAVNKVVKAIQRNRAGLKDPNRPIGTFIFLGSTGVGKTELAKVMARELFDSDEALIRIDMSEYMEKFAVSRLVGAPPGYVGYEEGGQLTEAVRRKPYAVVLLDEIEKAHPDVFNLLLQILDEGYVTDSLGRKIDFRNTIIILTSNIGTRDLKDFGDGVGFGTAARQSTSDARARATIESALKKAFAPEFLNRIDDIIIFNSLQKEDIRKIIDLELTKLYTRLNKLGYKLQLTDEAKDFIAEKGWDKDFGARPLKRVVQKYIEDLLAEMLVNKQIDEGEELLLSLNETKDALVKA
>NZ_CP029149.1|WP_120488223.1|920629_920875_+|uroporphyrinogen-decarboxylase
MNSQIAEYIGYTASIFIVLSFVFKNITTIRIINMIGCMCFVVYGFYSGDKPFYPVIIPNAILSVVQIFFLIKESKNKPSNS
>NZ_CP029149.1|WP_120488222.1|920876_921296_+|SufE-family-protein
MTIQEKQQEIINDFEFLEDWEQKYEYIIDLGKGLKPMAEDKKTEENLIKGCQSQVWISPDFREGKLYFDVDSDGILPKGIVALLASVYSGHPVEEILSSDFKFIEEIGLREFLSPSRANGLAAMTKQIKFYAVAYQLKS
>NZ_CP029149.1|WP_120489650.1|921295_922273_+|glycosyltransferase-family-9-protein
MKVVAYRFSALGDVAMTAPVFREILEQNPNLEITIVSRDSFRDIFEGIPRLNFKGVNLKKYKGLMGMRKLALEIHHEIKPDFIADLHDVIRSKMLNKIFKIKGYKVFKINKGKEEKKLLTDVWNIEKHPIKRTTERYADVFREMGFPVTLSDKLRPTSEAKHGIGIAPFAQHKGKVLPIEKTYELIKIIAKKEKVYLFGGGKEETEILSQWEKEIPNTHSLAGKLKLKEELQQIGELKLMISMDSANMHFASLMGTRCISIWGQTHPYAGFLGYGQRLEDAVHIQDLTCRPCSVFGDKECYRGDWACLHEINIQKILSKVYPQEV
>NZ_CP029149.1|WP_160224065.1|922414_923278_-|ferric-siderophore-ABC-transporter-substrate-binding-protein
MDYAELHRNNQTKDKRRSAVITALLTLLFFLLIYFYQFTRTLPKEEVITTMLINFGDNQNGTGEEEPAPQIPPNTVENIQPQPTPVSPPQPETKPQPQETVKDKILTGKNEKLIAEKPKETKKEVKSKEKTTTQNTDKATSSQSKTKQASSANTNSQPQPNEAVANLLRGRGTKAGSQGTAGTSGNEGDPLGGEGSGNSKIGVDRKLVAFIPGTMGRGGAQPAHDCTASGTITISYTVDKAGNVTSAHRLSGSSDPCIVSITISWIKRYVKAEKAQTSSTGTYSISF
>NZ_CP029149.1|WP_120488220.1|923315_923714_-|biopolymer-transporter-ExbD
MNLRRRNRVSAEFSMASMTDIIFLLLIFFMITSSAISQSAIDVKLPKASAGDPSIQDPTAITVKEDGSYFINDKEMKAEEIENYLVNLLKDEQNPAFTIRADENTKHKDIVFLMNIAETHHFNIAIATLQVD
>NZ_CP029149.1|WP_160224066.1|923718_924399_-|MotA/TolQ/ExbB-proton-channel-family-protein
MQDSLATGTVQLQSEKHIFSLWEILFSGGILGNTIMIAIFLLGVLSLYIFFERYFFIRRAAKEVPNFLENIKDFVQDGKIETAIDYCKTIDSPEARMIEKGLSRIGRPISDISNAMEAQGQVEVSKLEKNLNILASASGAAPMLGFLGTVVGMIMAFFEISNVTGAVSPKLLATGIYTAMATTAVGLFVGIPAYFFYNILVTNVDRLVLKIQTHTGEFLDTLNKPL

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Crispr_ID: NZ_CP029149_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP029149_5

988158-988244

Orphan

Consensus_repeat	Method
CTTAATAGATAAGCTAGATTGCGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP029149_5

>merge|NZ_CP029149|5|988158-988244|CRISPRCasFinder
CTTAATAGATAAGCTAGATTGCGGATGCCGTAGTCGGCACTACACATATTTACATTCATCTTACTTAATAGATAAGATAGATTGCGG

>NZ_CP029149|5|4|988158-988244|CRISPRCasFinder
CTTAATAGATAAGCTAGATTGCGG	ATGCCGTAGTCGGCACTACACATATTTACATTCATCTTA
CTTAATAGATAAGATAGATTGCGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP029149.1\|WP_120489848.1\|1001025_1001871_+\|gliding-motility-protein	unknown	unknown	gnl\|CDD\|224512
NZ_CP029149.1\|WP_160224099.1\|997741_998740_+\|glycosyltransferase	unknown	unknown	gnl\|CDD\|182223
NZ_CP029149.1\|WP_160224102.1\|1001877_1004370_+\|polysaccharide-biosynthesis-tyrosine-autokinase	unknown	unknown	gnl\|CDD\|349772
NZ_CP029149.1\|WP_120488168.1\|986580_987234_+\|CBS-domain-containing-protein	unknown	unknown	gnl\|CDD\|341419
NZ_CP029149.1\|WP_120488167.1\|987241_988111_+\|NAD-kinase	unknown	unknown	gnl\|CDD\|179352
NZ_CP029149.1\|WP_120488169.1\|985896_986433_+\|RNA-methyltransferase	unknown	unknown	gnl\|CDD\|349970
NZ_CP029149.1\|WP_160224098.1\|996446_997745_+\|branched-chain-amino-acid-transport-system-II-carrier-protein	unknown	unknown	gnl\|CDD\|283235
NZ_CP029149.1\|WP_160224101.1\|999878_1000988_+\|undecaprenyl/decaprenyl-phosphate-alpha-N-acetylglucosaminyl-1-phosphate-transferase	unknown	unknown	gnl\|CDD\|133463
NZ_CP029149.1\|WP_120488175.1\|979694_980702_+\|aspartate-semialdehyde-dehydrogenase	unknown	unknown	gnl\|CDD\|237845
NZ_CP029149.1\|WP_160224094.1\|980792_981785_+\|cation-transporter	unknown	unknown	gnl\|CDD\|223131
NZ_CP029149.1\|WP_160224095.1\|981794_983078_-\|sodium:proton-antiporter	unknown	unknown	gnl\|CDD\|223104
NZ_CP029149.1\|WP_120489852.1\|995225_996431_+\|GTPase-HflX	unknown	unknown	gnl\|CDD\|274455
NZ_CP029149.1\|WP_160224698.1\|1004620_1005433_+\|outer-membrane-beta-barrel-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_160224096.1\|983726_985397_+\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224055
NZ_CP029149.1\|WP_120488176.1\|979208_979664_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_120489846.1\|1005460_1006213_+\|isoprenyl-transferase	unknown	unknown	gnl\|CDD\|259850
NZ_CP029149.1\|WP_120488170.1\|985469_985802_+\|DUF3276-family-protein	unknown	unknown	gnl\|CDD\|378691
NZ_CP029149.1\|WP_120488172.1\|983138_983573_-\|ribose-5-phosphate-isomerase-B	unknown	unknown	gnl\|CDD\|376799
NZ_CP029149.1\|WP_160224097.1\|988489_989560_+\|class-II-fructose-bisphosphate-aldolase	unknown	unknown	gnl\|CDD\|236406
NZ_CP029149.1\|WP_160224100.1\|998806_999868_+\|EpsG-family-protein	unknown	unknown	gnl\|CDD\|379716

Protein	Function_ID	Function_description	E-value
NZ_CP029149.1\|WP_120489848.1\|1001025_1001871_+\|gliding-motility-protein	gnl\|CDD\|224512	COG1596, Wza, Periplasmic protein involved in polysaccharide export, contains SLBB domain of b-grasp fold [Cell wall/membrane/envelope biogenesis].	1.27967e-08
NZ_CP029149.1\|WP_160224099.1\|997741_998740_+\|glycosyltransferase	gnl\|CDD\|182223	PRK10073, PRK10073, putative glycosyl transferase; Provisional.	5.41591e-40
NZ_CP029149.1\|WP_160224102.1\|1001877_1004370_+\|polysaccharide-biosynthesis-tyrosine-autokinase	gnl\|CDD\|349772	cd05387, BY-kinase, bacterial tyrosine-kinase. Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on a C-terminal tyrosine cluster and also phosphorylate endogenous protein substrates by using ATP as phosphoryl donor. Besides their capacity to function as tyrosine kinase, most of these proteins are also involved in the production and transport of exopolysaccharides. BY-kinases are involved in a number of physiological processes ranging from stress resistance to pathogenicity.	3.51389e-56
NZ_CP029149.1\|WP_120488168.1\|986580_987234_+\|CBS-domain-containing-protein	gnl\|CDD\|341419	cd17783, CBS_pair_bac, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).	1.38236e-06
NZ_CP029149.1\|WP_120488167.1\|987241_988111_+\|NAD-kinase	gnl\|CDD\|179352	PRK01911, ppnK, inorganic polyphosphate/ATP-NAD kinase; Provisional.	1.58449e-117
NZ_CP029149.1\|WP_120488169.1\|985896_986433_+\|RNA-methyltransferase	gnl\|CDD\|349970	cd18097, SpoU-like, SAM-dependent rRNA or tRNA methylase related to SpoU. RNA 2'-O ribose methyltransferase catalyzes the methyltransfer from S-adenosyl-L-methionine (AdoMet) to the 2'-OH group of ribose in tRNA or rRNA. It is part of the SpoU family of MTases, a subfamily of the SPOUT methyltransferase superfamily. The SPOUT methyltransferase superfamily is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot.	1.01013e-68
NZ_CP029149.1\|WP_160224098.1\|996446_997745_+\|branched-chain-amino-acid-transport-system-II-carrier-protein	gnl\|CDD\|283235	pfam05525, Branch_AA_trans, Branched-chain amino acid transport protein. This family consists of several bacterial branched-chain amino acid transport proteins which are responsible for the transport of leucine, isoleucine and valine via proton motive force.	2.63513e-96
NZ_CP029149.1\|WP_160224101.1\|999878_1000988_+\|undecaprenyl/decaprenyl-phosphate-alpha-N-acetylglucosaminyl-1-phosphate-transferase	gnl\|CDD\|133463	cd06853, GT_WecA_like, This subfamily contains Escherichia coli WecA, Bacillus subtilis TagO and related proteins. WecA is an UDP-N-acetylglucosamine (GlcNAc):undecaprenyl-phosphate (Und-P) GlcNAc-1-phosphate transferase that catalyzes the formation of a phosphodiester bond between a membrane-associated undecaprenyl-phosphate molecule and N-acetylglucosamine 1-phosphate, which is usually donated by a soluble UDP-N-acetylglucosamine precursor. WecA participates in the biosynthesis of O antigen LPS in many enteric bacteria and is also involved in the biosynthesis of enterobacterial common antigen. A conserved short sequence motif and a conserved arginine at a cytosolic loop of this integral membrane protein were shown to be critical in recognition of substrate UDP-N-acetylglucosamine.	3.25178e-65
NZ_CP029149.1\|WP_120488175.1\|979694_980702_+\|aspartate-semialdehyde-dehydrogenase	gnl\|CDD\|237845	PRK14874, PRK14874, aspartate-semialdehyde dehydrogenase; Provisional.	1.74254e-171
NZ_CP029149.1\|WP_160224094.1\|980792_981785_+\|cation-transporter	gnl\|CDD\|223131	COG0053, MMT1, Predicted Co/Zn/Cd cation transporters [Inorganic ion transport and metabolism].	2.12602e-57
NZ_CP029149.1\|WP_160224095.1\|981794_983078_-\|sodium:proton-antiporter	gnl\|CDD\|223104	COG0025, NhaP, NhaP-type Na+/H+ and K+/H+ antiporters [Inorganic ion transport and metabolism].	1.32208e-70
NZ_CP029149.1\|WP_120489852.1\|995225_996431_+\|GTPase-HflX	gnl\|CDD\|274455	TIGR03156, GTP_HflX, GTP-binding protein HflX. This protein family is one of a number of homologous small, well-conserved GTP-binding proteins with pleiotropic effects. Bacterial members are designated HflX, following the naming convention in Escherichia coli where HflX is encoded immediately downstream of the RNA chaperone Hfq, and immediately upstream of HflKC, a membrane-associated protease pair with an important housekeeping function. Over large numbers of other bacterial genomes, the pairing with hfq is more significant than with hflK and hlfC. The gene from Homo sapiens in this family has been named PGPL (pseudoautosomal GTP-binding protein-like). [Unknown function, General].	1.79045e-176
NZ_CP029149.1\|WP_160224096.1\|983726_985397_+\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|224055	COG1132, MdlB, ABC-type multidrug transport system, ATPase and permease components [Defense mechanisms].	2.97478e-134
NZ_CP029149.1\|WP_120489846.1\|1005460_1006213_+\|isoprenyl-transferase	gnl\|CDD\|259850	cd00475, Cis_IPPS, Cis (Z)-Isoprenyl Diphosphate Synthases. Cis (Z)-Isoprenyl Diphosphate Synthases (cis-IPPS) catalyze the successive 1'-4 condensation of the isopentenyl diphosphate (IPP) molecule to trans,trans-farnesyl diphosphate (FPP) or to cis,trans-FPP to form long-chain polyprenyl diphosphates. A few can also catalyze the condensation of IPP to trans-geranyl diphosphate to form the short-chain cis,trans- FPP. In prokaryotes, the cis-IPPS, undecaprenyl diphosphate synthase (UPP synthase), catalyzes the formation of the carrier lipid UPP in bacterial cell wall peptidoglycan biosynthesis. Similarly, in eukaryotes, the cis-IPPS, dehydrodolichyl diphosphate (dedol-PP) synthase catalyzes the formation of the polyisoprenoid glycosyl carrier lipid dolichyl monophosphate. cis-IPPS form homodimers and are mechanistically and structurally distinct from trans-IPPS, which lack the DDXXD motifs, yet require Mg2+ for activity.	6.1125e-129
NZ_CP029149.1\|WP_120488170.1\|985469_985802_+\|DUF3276-family-protein	gnl\|CDD\|378691	pfam11680, DUF3276, Protein of unknown function (DUF3276). This bacterial family of proteins has no known function.	4.85362e-39
NZ_CP029149.1\|WP_120488172.1\|983138_983573_-\|ribose-5-phosphate-isomerase-B	gnl\|CDD\|376799	pfam02502, LacAB_rpiB, Ribose/Galactose Isomerase. This family of proteins contains the sugar isomerase enzymes ribose 5-phosphate isomerase B (rpiB), galactose isomerase subunit A (LacA) and galactose isomerase subunit B (LacB).	2.04185e-73
NZ_CP029149.1\|WP_160224097.1\|988489_989560_+\|class-II-fructose-bisphosphate-aldolase	gnl\|CDD\|236406	PRK09197, PRK09197, fructose-bisphosphate aldolase; Provisional.	0
NZ_CP029149.1\|WP_160224100.1\|998806_999868_+\|EpsG-family-protein	gnl\|CDD\|379716	pfam14897, EpsG, EpsG family. This family of proteins are related to the EpsG protein from B. subtilis. These proteins are likely glycosyl transferases belonging to the membrane protein GT-C clan.	4.56934e-22

>NZ_CP029149.1|WP_120488167.1|987241_988111_+|NAD-kinase
MKKVAAIYTQKKDLNTFLYLSKFISELDKRKVRAVIYSAAAEAMEFSHQFETFETKTDLLDKGVDIFFTFGGDGTIVNSLLFIEDTEIPVVGVNTGRLGFLASFTKEEIFKQLDEVLRGDINISKRSVIEVVQPKGDFFPYALNDITISRRETTSMITVDSQLDDEFLNIFWGDGLIVSTPTGSTAYSLSCGGPILSPDNKNFVVTPIAPHNLNVRPLVVSDSVELKFKVSSRVPQYSISLDSRLIHLDTDTEIVIRKASFKMKLIQPKHLNFYDTIRQKLLWGKDKRN
>NZ_CP029149.1|WP_120488168.1|986580_987234_+|CBS-domain-containing-protein
MFVKDYISKDYPAFDEKTQVREILPLADDFGYSHLFVERAGVFVGALSRSFLNDAPEGRLKDLEIHFEKFAIREDAFLIDIVKLFYTFNANVVPILAESENYLGYISCDDVFDEFSKYPLFSENGAVILLQTYNKHYSFAEITRIVEENNAKIYGIYVSDINEDEVKITLKISNHHLSNIEEDLERFGYSIINKDYNDRKESLVKNRFDFFQKYIEI
>NZ_CP029149.1|WP_120488169.1|985896_986433_+|RNA-methyltransferase
MTQKLKLEELGRVDVQTFKGLAKIPLVIVLDNIRSMHNVGAVFRTADAFLIEKVILCGITPRPPHREIHKAALGATESVDWLYYESVKEAALDLKIQKYDVLGIEQTTDSIMISDYEINPQRKYALVLGNEVEGISDEILNHCNAFIELPQHGTKHSLNVSVCGGIVMWDFYKALYKK
>NZ_CP029149.1|WP_120488170.1|985469_985802_+|DUF3276-family-protein
MSEYKERHENEIFTKVLKAGRRTYFFDVRETKAGDYYLTITESKKSFSDSGEASFEKHKIYLYKEDFKGFLELFKESTEFIVSEKGEDVISEKHDKDFKSRYTINNEEEI
>NZ_CP029149.1|WP_160224096.1|983726_985397_+|ABC-transporter-ATP-binding-protein
MKALNTLNPYFWKHRTLLFFGLLFILASNFFMIYKVQFVGRAVDELAESGKLGFNAEILKYVAIYVVASLLTGFFTFMMRQTIIVASRKIEYELKNKIYQHYQQISVTDFKRTTIGDLMNRLSEDVVAIRMYLGPGVMYVVNLAVLVIITSIYMLKTDLTLTLWALLPFPFLSYTIYKVSSIINAKSKRMQKSQSEISTFVTDSFSGIRVIKFFAKEIYINSGYVSRVKEYQDKALNLAKTEAVFYTVILFVIGLINVMVLYVGGIKYMAGEISVGKIADFFLYVNTLIWPFSLVGWITSVNQRAEASMQRVNEFLNMKSEIINTNFNEYPIKGDIEFQNVSYVYPNTGIKALDNLSFKLSAGDSLAIMGKTGCGKTTLALLLCRLIDPTEGEILIDGKNLKEHNLDLYRKHIGYVPQENYLFSDTIESNIGFALDEPNHQKVVHYAKVADIHKNIETFKEGYQTMVGERGVMLSGGQKQRVCIARALIKEPDILIFDDSLSALDNETEKNILQNIEQEAKNRTLIIITHRMSSAEKANKILNLSAETNEYSAEIN
>NZ_CP029149.1|WP_120488172.1|983138_983573_-|ribose-5-phosphate-isomerase-B
MIKLAIACDHAGFEYKEYLKKELSAQFEITDYGTHSAASVDYPDFVHPAAISVEKGENQFGILVCGSGQGVQLTANKHAGIRCALCWMPELGALARQHNNCNMLALPARFIAKELSLEIAKTFLSTPFEGGRHQSRVDKISAGC
>NZ_CP029149.1|WP_160224095.1|981794_983078_-|sodium:proton-antiporter
MELYYSFSILIVLATMFEYINHKLLRLPSTIGVMVIAICVSIILILFGESLLPKTTLSLHKIVSSVDFTEVLMGAMLNFLLFAGGIHINIKDLREQIAPVVMFASIGVVISTFAVGFGAYYLLPFAGVEIPLIYCLVFGALISPTDPVAVLSILKKAKVSKSLETKVAGESLFNDGVAIVVFTVLLQIAVGKQVDLTLESILMLVVQEAGGGLLLGAVLGFIGSKMMQNTNDYILSVLITLSIVMGGYLIAHSMHISGPLTMVAAGLFMGNFSPKFKMKSEVRDYLVKFWELIDEIMNAVLFLFIGLELLLIKNLNEYLFAGGICILVVLLARWVSIFFPTKLMSFKHRFTPQTVKVLVWGGLRGGVSIALALSIPKSEYNHIIISITYCVVVFSIIFQGLTIDKIANPKKIAQEETKQEELEEMKN
>NZ_CP029149.1|WP_160224094.1|980792_981785_+|cation-transporter
MKEQAINKKNFSFQRSVAIIGVLLFIGKLITWQITASDAVFSDAMESIVNIVAAFMGLYSLYVASKPMDKDHPYGHGKIEFITSGIEGALIIFAGVVIIIQAVSSFIAKNTLHQLDWGILIIALTAVINYLMGYISYQKGVRENSLVLQSSGKHLQSDTLTTIGVVLSLVVVHFTHFYWIDALVAGIFGGYIIITGYKIIRESMKGIMDEADTKIITDIAEFLNEHRKPEWIDVHNMKIQQFGSHLHIDAHLTLPWYFELRQAHNEMEELIISIAENTDREIEFNFHMDDCKPSSCEVCQIMDCPVRKLPFVKKIDWTVETITQTGKHKL
>NZ_CP029149.1|WP_120488175.1|979694_980702_+|aspartate-semialdehyde-dehydrogenase
MKIAVVGATGMVGQVMLKVLEERNFPVTELIPVASEKSVGKSVHFKGEEYTLVSIQSAVEQKPEIAIFSAGGATSLEWAPKFAEMGTFVIDNSSAWRMDATKKLVVPEINASEITKDDKIIANPNCSTIQLVMVLHPLHKKYGLKRVVVSTYQSVTGTGKAAVDQLQDEVKSSVTAQDCTVPKVYPYEIFKNALPQCDVFSDEGYTKEELKLMREPKKIMSDDSFQLTATAVRVPVQGGHSESVNIEFHQDFNLDEVREILSHTKGVTVQDDVEKSLYPMPLYSEGKDEVFVGRIRRDPSQPKTLNCWIVADNLRKGAATNAVQIAEHLVKQKLV
>NZ_CP029149.1|WP_120488176.1|979208_979664_+|hypothetical-protein
MGKLHFILTKAHGGFAYIELILVLVFLVALFAVMFGYSGRVTKLLRKSTLFVMIFFHIQLIVGFVMLIGTSEFLNTIKAVGMGKIMKDAYLRQSFVEHPTSMLIAAILMTIVNKKIKKAGHLSMSAFWLSVLAILFFGFAFSIVMGRLFGA
>NZ_CP029149.1|WP_160224097.1|988489_989560_+|class-II-fructose-bisphosphate-aldolase
MSRIFPAGVATGNLVTEIFQHAKENNYALPAVNVIGSSNVNATMETAAKLNSPVIIQFSNGGAAFNAGKGLSNDAQKAAILGAVAGAKHIHTLAEAYGATVILHTDHCAKKLLPWVDGLLDANEEYYKKFGKTLYSSHMLDLSEESLQENLDISCEYFKRMAKLNMTLEVEIGVTGGEEDGVDNSDVDNSKLYTQPEDVAYTYERLKAISPNFTIAAAFGNVHGVYKPGNVVLTPKILDNSQKFVKEKLHTEDKPVNFVFHGGSGSTLEEIREAISYGVVKMNIDTDLQFAYTEGVRDYMLDKIEYLRSQIGNPEGDDKPNKKFYDPRVWLRKGEETFVKRLVRSFEDLNNVGTLG
>NZ_CP029149.1|WP_120489852.1|995225_996431_+|GTPase-HflX
MIERKEHRYEKAVLVGLITREQDEDKLTEYLDELEFLAYTAGASVERRFTQKLTQADSRTFVGKGKMEEIRDFVRENEIGTVIFDDELSPSQLKNLEREMEVKILDRTNLILDIFAQRAQTSYARTQVELAQYEYLLPRLTRMWTHLERQRGGIGMRGPGETEIETDRRIIRDRIALLKEKLKTIDKQMATQRNNRGKMVRVALVGYTNVGKSTLMNALSKSDVFAENKLFATLDTTVRKVVIGNLPFLLTDTVGFIRKLPTQLVESFKSTLDEVREADLLLHIVDISHESFEDHINSVHQILQEIDAHQKPMIMVFNKIDGFSYVKKDEDDLTPAKRENISLDEWKKTWMAKSKYPTVFISALTKENFPEMKKMIYDEVHRIHISRFPYNDFLFEYFDEE
>NZ_CP029149.1|WP_160224098.1|996446_997745_+|branched-chain-amino-acid-transport-system-II-carrier-protein
MKQKNKWITITTVGFALFAMFFGAGNLIIPPFIGLYTGEDWWLGLLGFFITAIFAPFLGVMMVAVTGNTFTDLGKKLPPVLINSLALLIILCIGPIIAIPRTGATTYEVGFKPFFPEMNSLVFSVVFFALVFVLSISKTKIVDVIGKVLTPFLLLALVLLILMGVMSPVKEPLIEGESLMESFKLGFTEGYQTLDVLASVIFAGLIISGVINSGYTTEHEKTNITIWAGVVSTVALLFVYGGLIYLGAMTDYQTEGDVARSELLLYISKSVLGHNGTFVISVAISLACLTTAIALTSATGAFFENISKGRISYRIAVAVCSIVSLILSVNSVEEIINYAADILIFIYPVTFTLLLLILVFGRKVDYKLPYVLGMLMTAFLSLISVFENMKWDFERLYHLKKSIPLSSYNLEWLLPSVIAFWVGYIISKISQK
>NZ_CP029149.1|WP_160224099.1|997741_998740_+|glycosyltransferase
MKKVSVIVPVYNVEKYLEKCLNSLVCQSLEAIEIIVVNDGSTDNSQAIIDGFNEKYPDKIKSFTKENGGLSDARNFGIERAEGEFIGFVDSDDYVSVEMFEEMYHLAKKHDAEMVICNLQKVDENGNVTQKLTQIPNMPEKINLETEFSVFSDLSYFACNKIFKKKLFDNKKFKKGIHFEDIQLIPQLLLSCKTIAQTQKYHYQYLERQDSITKTHTEKGLDILRAVEDVEQTFYTSVYSHKLKELKGFQILEGIYSFLAYLAFVKDTSTYQKMSLELKKFIKDRGISRREILGYKRFDTNYILSLPLKKKIYYFLYFFNQERIINFILKKN
>NZ_CP029149.1|WP_160224100.1|998806_999868_+|EpsG-family-protein
METYASDYKNYKGVWVVIVFLIILSGLREDAGADYGVYAIMYRDFGVSIDYSELLEGTLFRENKLPIEWLYSVIGKVFFSFGLPFFIFTLFLAIVSVGIKYLAFEQSVVYPALSMLLYLFPSYFTGDSGHMRQAFAMGILMFSFLFIKKRNLLMFLIMVYLAMGFHKSSAVFVLAYWIAIVPMNRITLLGMVLISVLLSPFQVYNYISIFESLAPVEVYSGFSAYSTIEGDTSTIKFTDLISIMYMFFVYFYDKDACKQIPYYEYMRNIGVFGICLYFIFRGSPIFSGRLAAIYLVFMVMVIPNIIAAIKNLQLRRGLHFIVIAYVVFYCIVYTVMQGQRAGFTIEHYRNYLW
>NZ_CP029149.1|WP_160224101.1|999878_1000988_+|undecaprenyl/decaprenyl-phosphate-alpha-N-acetylglucosaminyl-1-phosphate-transferase
MDKIEIILNSIGISIFYIKLSMSFILSFLICFVSIPTIIKISRRKNLMDEPGDRSSHLRKIPNLGGVALFLSIAVCASVFAYELFDLYKFLFASLVILLYIGVMDDIMVLRAYKKLLVQVIVSVLIVIGSDVRIRSLFGVFGVYELNYFLSVVFSVITFIILINAFNLIDGIDGLAGAYSVLCSLFFGVSYYRLGVYNYPLVILSVIIIGAVLAFLYYNLSPYRSIRIFMGDTGSMILGFLLAFTAICFIDIFIDKDIRYLPRYHLNSAPVVAVAILILPIIDTLNVIIIRLSQKKSPFEADKNHIHHRLLALGISHRRATFYIISYYCFIVGITYWLRHLENNLLLSIIVILGFIGAYIPVWLLKLKK
>NZ_CP029149.1|WP_120489848.1|1001025_1001871_+|gliding-motility-protein
MNIKHLLFYTFILTVLTSCITTKDIKYLQPNENLVINEEGLVPYNIQEYRVTKNDIFNLNIVTTSKGDAAQFYSMFNTSGGINSGNSVNQVYNNNNANDNVRFYFNGIKVDSNGEIYILGIGYLKAEGRTIEDIRNEIQQKVNENFLKDKTDVRLNLDGITYYVLGDIETVGVSGKKTAYTQTLSITEALSLDGGLNRTVDKKDVIIHRRYPEGIKIVKLDLTREDVMNSPYYWIQNGDMIYLNTRKKSLNGFGKDPLNTLTTGVTLLTTALSVYLLISRL
>NZ_CP029149.1|WP_160224102.1|1001877_1004370_+|polysaccharide-biosynthesis-tyrosine-autokinase
MIPNKETNKKGNNENASQESIASFSLFDAGLFIQKLIRNWYWFVFMFGVGYVIAYVYSRYFTQRIYESNLSLSMSSNATSYFTPNQSINFIWDQRSNSDGLFLKKMILSRSHNEYLVKKLDLFVNYSTKGVIKETYLDKYDSPVFIEIDRDYPQQINFPITLLPKGNDQYEVTFPEEGFSNYLYNYKNETFVSVPEYPVPQNKLIKVGQWYTAPNFKFKLVKNPVTPAIGVDNIIIKLSSVNAAVQSIIATTSVKFDEELNSVIIISKRGYNLNGTVQFLNTTVEELIKKRLEDRNTVDQNTVKYLTVNLERVKKQLDSAATKLNDIKLKEGIFNLEEGDTRIWGSITDLEKKKVDIQDKIKTLNNIKRTLMSSSLDNLISLRSAGIDDSSFSTTVSELKLLYIKKREMESIYTPQSEAMKEINRQINDIKLGSQANLQSYYDDFYKELNEINQKISQAENSLVNLPEGQRRYFDVKRGYDIIENTYSLLLTKQAESKMRVATNRSDLNIIDPAKNLDQGPVAPNISNIKNIIIGVLLLIPLLIIVLRTLLDNRVINIKEVLRVTKIPLLGVIGKSSHENNLTVLEQPKSSVSEAFRGLRANLRFLAGEDGRAKVILVTSSISGEGKTYTAINIASVLGLSGKKTILLGMDLRKPKIFGDFKIDNRYGLSNYLTGEVGMGDIINKTEISSLDVITSGPIPPNPSELLMSQKNIDFIQGLREHYDFIIIDSPPVGLVADSFELMKYTDANIYVVRHEYTEKYMLKMITEKYAKHEIQHLGLVYNDYQVKQGYGYGYGYGYGYGYGYFDEDANYKEPTLIRLRNKIKSILRK
>NZ_CP029149.1|WP_160224698.1|1004620_1005433_+|outer-membrane-beta-barrel-protein
MATFFSFLSFGQRHEIGLKLGLSSVVGDIGQDNYQLNAPVFSKISSYGVPFHIEAMYRMNFNPYQTLRIDAGYFQVQFDDEYADEAYRNKRRKGNSNNGGNLDVVFEYNFFPVNNEQSSMLSPYIFGGIGGLVTNTPYLRIKDKSQGAAAASPDFEIYETRKGKFIMSIPFGVGIKYKFHYNWAASAEVKFRPTFSDGIDYSTLSRKDVGTVFNNELRKKNPKVYDEAIDKEVEKYMKDRNIGNTNSNDWLNSVMIGLSYSFGRPPCYCD
>NZ_CP029149.1|WP_120489846.1|1005460_1006213_+|isoprenyl-transferase
MKSYKEIINPEKLPQHVAIIMDGNGRWAKSRGEERTYGHRNAIDAVRNAINACNEVNIPYLTLYTFSSENWNRPDDEVSTLMSLLSETLLTEADEIFTKGLRMHMIGDISRLPELVREQLLNVIDLTKNNTKGNLILALNYGSQREILKAVKEISQEVKDGQLQIEDITEAVFEKHLYTKDFPPVDLMIRTSGEVRISNFLLWQLAYAELQFLDVLWPDFSKEDFFKCIVDYQKTERRYGKTSEQIALSN

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Crispr_ID: NZ_CP029149_6

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP029149_6

1089706-1089838

Orphan

Consensus_repeat	Method
TGGTTCAGAGCATCTGGTTTACACCCAGAGGGTCGGGGGTTCGAATCCCT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP029149_6

>merge|NZ_CP029149|6|1089706-1089838|CRISPRCasFinder
TGGTTCAGAGCATCTGGTTTACACCCAGAGGGTCGGGGGTTCGAATCCCTCACCGCCCACCGAGCAAGGGTTCTTAGCTCAGCTGGTTCAGAGCATCTGGTTTACACCCAGAGGGTCAGGGGTTCGAATCCCT

>NZ_CP029149|6|5|1089706-1089838|CRISPRCasFinder
TGGTTCAGAGCATCTGGTTTACACCCAGAGGGTCGGGGGTTCGAATCCCT	CACCGCCCACCGAGCAAGGGTTCTTAGCTCAGC
TGGTTCAGAGCATCTGGTTTACACCCAGAGGGTCAGGGGTTCGAATCCCT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP029149.1\|WP_120489779.1\|1085309_1086335_+\|rod-shape-determining-protein	unknown	unknown	gnl\|CDD\|237562
NZ_CP029149.1\|WP_160224146.1\|1087886_1088279_+\|tetratricopeptide-repeat-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_160224151.1\|1095054_1095942_-\|glycosyltransferase	unknown	unknown	gnl\|CDD\|133055
NZ_CP029149.1\|WP_160224148.1\|1091274_1092180_+\|hydroxymethylbilane-synthase	unknown	unknown	gnl\|CDD\|234612
NZ_CP029149.1\|WP_160224150.1\|1093930_1094659_+\|tRNA-threonylcarbamoyladenosine-dehydratase	unknown	unknown	gnl\|CDD\|238384
NZ_CP029149.1\|WP_160224152.1\|1095963_1097034_+\|glycosyltransferase	unknown	unknown	gnl\|CDD\|340839
NZ_CP029149.1\|WP_120489775.1\|1090010_1091288_+\|glutamyl-tRNA-reductase	unknown	unknown	gnl\|CDD\|234592
NZ_CP029149.1\|WP_160224144.1\|1083495_1084377_-\|NifU-family-protein	unknown	unknown	gnl\|CDD\|378032
NZ_CP029149.1\|WP_160224143.1\|1081940_1082351_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_160224145.1\|1084527_1085064_+\|gamma-carbonic-anhydrase-family-protein	unknown	unknown	gnl\|CDD\|100051
NZ_CP029149.1\|WP_120489767.1\|1098193_1098586_+\|WxcM-like-domain-containing-protein	unknown	unknown	gnl\|CDD\|377522
NZ_CP029149.1\|WP_160224703.1\|1082419_1083454_-\|ferrochelatase	unknown	unknown	gnl\|CDD\|234585
NZ_CP029149.1\|WP_160224702.1\|1079953_1081750_+\|elongation-factor-4	unknown	unknown	gnl\|CDD\|235462
NZ_CP029149.1\|WP_120489777.1\|1087213_1087720_+\|rod-shape-determining-protein-MreD	unknown	unknown	unknown
NZ_CP029149.1\|WP_120489770.1\|1094655_1095003_+\|ribonuclease-P-protein-component	unknown	unknown	gnl\|CDD\|234989
NZ_CP029149.1\|WP_160224147.1\|1088412_1089657_+\|bifunctional-folylpolyglutamate-synthase/dihydrofolate-synthase	unknown	unknown	gnl\|CDD\|223362
NZ_CP029149.1\|WP_160224149.1\|1092180_1092861_+\|uroporphyrinogen-III-synthase	unknown	unknown	gnl\|CDD\|376850
NZ_CP029149.1\|WP_120489778.1\|1086358_1087207_+\|rod-shape-determining-protein-MreC	unknown	unknown	gnl\|CDD\|237560
NZ_CP029149.1\|WP_120489772.1\|1092883_1093909_+\|uroporphyrinogen-decarboxylase	unknown	unknown	gnl\|CDD\|234644
NZ_CP029149.1\|WP_160224153.1\|1097030_1098110_+\|glycosyltransferase-family-4-protein	unknown	unknown	gnl\|CDD\|340847

Protein	Function_ID	Function_description	E-value
NZ_CP029149.1\|WP_120489779.1\|1085309_1086335_+\|rod-shape-determining-protein	gnl\|CDD\|237562	PRK13927, PRK13927, rod shape-determining protein MreB; Provisional.	0
NZ_CP029149.1\|WP_160224144.1\|1083495_1084377_-\|NifU-family-protein	gnl\|CDD\|378032	pfam08712, Nfu_N, Scaffold protein Nfu/NifU N terminal. This domain is found at the N-terminus of NifU and NifU related proteins, and in the human Nfu protein. Both of these proteins are thought to be involved in the the assembly of iron-sulphur clusters.	7.74851e-24
NZ_CP029149.1\|WP_160224151.1\|1095054_1095942_-\|glycosyltransferase	gnl\|CDD\|133055	cd06433, GT_2_WfgS_like, WfgS and WfeV are involved in O-antigen biosynthesis. Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.	2.9071e-28
NZ_CP029149.1\|WP_160224148.1\|1091274_1092180_+\|hydroxymethylbilane-synthase	gnl\|CDD\|234612	PRK00072, hemC, porphobilinogen deaminase; Reviewed.	5.6941e-105
NZ_CP029149.1\|WP_120489772.1\|1092883_1093909_+\|uroporphyrinogen-decarboxylase	gnl\|CDD\|234644	PRK00115, hemE, uroporphyrinogen decarboxylase; Validated.	1.7386e-173
NZ_CP029149.1\|WP_160224152.1\|1095963_1097034_+\|glycosyltransferase	gnl\|CDD\|340839	cd03811, GT4_GT28_WabH-like, family 4 and family 28 glycosyltransferases similar to Klebsiella WabH. This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.	4.63758e-63
NZ_CP029149.1\|WP_160224145.1\|1084527_1085064_+\|gamma-carbonic-anhydrase-family-protein	gnl\|CDD\|100051	cd04645, LbH_gamma_CA_like, Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.	3.24068e-73
NZ_CP029149.1\|WP_120489767.1\|1098193_1098586_+\|WxcM-like-domain-containing-protein	gnl\|CDD\|377522	pfam05523, FdtA, WxcM-like, C-terminal. This family includes FdtA from Aneurinibacillus thermoaerophilus, which has been characterized as a dtdp-6-deoxy-3,4-keto-hexulose isomerase. It also includes WxcM from Xanthomonas campestris (pv. campestris).	1.98465e-66
NZ_CP029149.1\|WP_160224703.1\|1082419_1083454_-\|ferrochelatase	gnl\|CDD\|234585	PRK00035, hemH, ferrochelatase; Reviewed.	4.62585e-132
NZ_CP029149.1\|WP_160224702.1\|1079953_1081750_+\|elongation-factor-4	gnl\|CDD\|235462	PRK05433, PRK05433, GTP-binding protein LepA; Provisional.	0
NZ_CP029149.1\|WP_160224150.1\|1093930_1094659_+\|tRNA-threonylcarbamoyladenosine-dehydratase	gnl\|CDD\|238384	cd00755, YgdL_like, Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli hypothetical protein ygdL. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of the substrate. The exact function of this family is unknown.	1.31568e-100
NZ_CP029149.1\|WP_120489770.1\|1094655_1095003_+\|ribonuclease-P-protein-component	gnl\|CDD\|234989	PRK01903, rnpA, ribonuclease P protein component.	5.41251e-16
NZ_CP029149.1\|WP_160224147.1\|1088412_1089657_+\|bifunctional-folylpolyglutamate-synthase/dihydrofolate-synthase	gnl\|CDD\|223362	COG0285, FolC, Folylpolyglutamate synthase [Coenzyme metabolism].	3.90791e-117
NZ_CP029149.1\|WP_160224149.1\|1092180_1092861_+\|uroporphyrinogen-III-synthase	gnl\|CDD\|376850	pfam02602, HEM4, Uroporphyrinogen-III synthase HemD. This family consists of uroporphyrinogen-III synthase HemD EC:4.2.1.75 also known as Hydroxymethylbilane hydrolyase (cyclizing) from eukaryotes, bacteria and archaea. This enzyme catalyzes the reaction: Hydroxymethylbilane <=> uroporphyrinogen-III + H(2)O. Some members of this family are multi-functional proteins possessing other enzyme activities related to porphyrin biosynthesis, such as HemD with pfam00590, however the aligned region corresponds with the uroporphyrinogen-III synthase EC:4.2.1.75 activity only. Uroporphyrinogen-III synthase is the fourth enzyme in the heme pathway. Mutant forms of the Uroporphyrinogen-III synthase gene cause congenital erythropoietic porphyria in humans a recessive inborn error of metabolism also known as Gunther disease.	1.3159e-32
NZ_CP029149.1\|WP_120489778.1\|1086358_1087207_+\|rod-shape-determining-protein-MreC	gnl\|CDD\|237560	PRK13922, PRK13922, rod shape-determining protein MreC; Provisional.	1.67748e-52
NZ_CP029149.1\|WP_120489775.1\|1090010_1091288_+\|glutamyl-tRNA-reductase	gnl\|CDD\|234592	PRK00045, hemA, glutamyl-tRNA reductase; Reviewed.	3.15904e-97
NZ_CP029149.1\|WP_160224153.1\|1097030_1098110_+\|glycosyltransferase-family-4-protein	gnl\|CDD\|340847	cd03820, GT4_AmsD-like, amylovoran biosynthesis glycosyltransferase AmsD and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.	2.75071e-70

>NZ_CP029149.1|WP_160224147.1|1088412_1089657_+|bifunctional-folylpolyglutamate-synthase/dihydrofolate-synthase
MNEKDYQEAIDWLFVQAPNYQINGKKAYKPGLENIRRLCDFFGNPQEKIKTIHIGGTNGKGSTSNMLASVLQQSGYKVGLFTSPHLIDFTERIKINGNNCDKTFVFGFIQKLKNLPKDDIKPSFFEYTTIMAFDYFYKNQVDFAIIEVGLGGRLDSTNIILPMLSAITNISLDHQDILGETLEQIAQEKAGIIKPDIPIVCGSDDAIVKEIIRKIADENRSPFIDATERDSPFTTDLKGRYQQKNIRVVLSLIDVLKDLGIIITEEDIAAGLMNVQKNTGFIGRWYEFSRAPLTICDTGHNQAGLEEVFSQLCSMPVFKHIILGFVNDKKIDKVLSILPKNACYYFVKPSVERGRHPKDYEDLLKAQQISYHLFDSVNDGYTAALKSCKKDEMIFIGGSNFVVGDFLKENLEGK
>NZ_CP029149.1|WP_160224146.1|1087886_1088279_+|tetratricopeptide-repeat-protein
MSSSCILHIKEAWELKTKSGDKLMKSGNYKEALEFYKEALYRAEVLNLHTYACRSIKVSFMSLLVSSFKNIIHIYERMNCIEQAEEMMKKMIAYIIKLFKNKEITEQEYQTEIKVALVSYTDFINKYQLK
>NZ_CP029149.1|WP_120489777.1|1087213_1087720_+|rod-shape-determining-protein-MreD
MITRNIFSDIIFISVLAVFQVVVLSRVNILGEYTPVMYPMFVMFYPFFRNKYIFLLLSFLLGFVIDANIGTWGVNAFATTLIAYFRTIIFRTSTDSDTDFFSFQSIQWSQFIFFILMSVFLHQFIVQFLEYFKLSRAVDILINVCITSIISFFFILVYAIAFRIKEKV
>NZ_CP029149.1|WP_120489778.1|1086358_1087207_+|rod-shape-determining-protein-MreC
MGILLRFFSKNSLFLFFLFLQIISLSLMFCMNTMQRSWIAAQSAAFNAWIAGYIDEGASYLKLKQANEELIKQNKELMEQLYGREYSSSSKPRVIADSTQGKQMFTIIDGDVINNSINRKNNYFTINRGSKDGVEDDMGVISPNGVVGIVVNTTAHYSLAQSVLSVDKIKINASLKNSGYFGTLTWNGEDSRLMHLADIPKYVSLKVGDTVVTDGKSAIFPQGKMIGTVAGFEVDNKTGFWDISVELSEKIGKLSKVFIVKNLKREEMKPIQDSLMKHQKAE
>NZ_CP029149.1|WP_120489779.1|1085309_1086335_+|rod-shape-determining-protein
MGLFDVFTQEIAIDLGTANTLIIHNNKIVIDQPSIVAIDRNTGKPIAVGEPAKHMQGKTHEDIKTIRPLKDGVIADFQASEHMIREFIKQIPAVKGKLFQPALKIVICIPSGITEVEKRAVKDSAQKVNAKEVRLIYEPMAAAIGVGIDVQKPEGNMIVDIGGGTTEIAVVSLGGIVCDKSVKIAGDVFNNDIAYYLRTHHNLYIGEKTAERIKIEAGSATEDLDVELEDISVQGRDLITGKPKEIMINYREIARALDKSIIRIEDAVMETLSMTPPELAADIWKTGIYLAGGGALLRGLADRLHKKTGLPVFVAEDPLRAVVRGTGIALKNMDKFNFLIG
>NZ_CP029149.1|WP_160224145.1|1084527_1085064_+|gamma-carbonic-anhydrase-family-protein
MALIKDVLGKSPVIGKGTYLAETATVIGDVQMGENCSVWFNAVIRGDVHYIKIGSKVNIQDNVMLHCTYQKSPLSIGNNVSIGHNAIVHGCTIKDNVLIGMGAIVMDDCIIEEKSIVGAGSVVTKGTHIKSGEVWGGIPAKKIKDINAELLENEIHRIADSYIKYASWYTLTGGTFIK
>NZ_CP029149.1|WP_160224144.1|1083495_1084377_-|NifU-family-protein
MLNVHIEPTENANVTKFVVDYTLIPGGLELHRDSDISEIPLAQELFKYPFISSIFITANFIAVEKADSVDWESVAESLREVIQDELLANPRIYRQTKRKELFPIYAEMTPNPNVMKFVSPKLILDGFIEVKVENRTPDVPLAEAIYNEFDFVTQVFVSDNFVAVTRNSSVEWHEVMNAVRSVIAEYLQDGGKVTHIEPQKHESPVEKIIERDYTEKEQKIADVLAQYVAPAVENDGGKISLIDYDEENKVAKMLLQGACSGCPSSRITLKNGIENILKQFLPDLVEVVEAVNG
>NZ_CP029149.1|WP_160224703.1|1082419_1083454_-|ferrochelatase
MMRRGILLVNLGSPKSTSVEDVKEYLDEFLMDERVIDYRWFFRYLLVRGIILKTRPAKSAEAYKTIWTSEGSPLIVYTEKIKTKLQQKVDMPVEIGMRYAEPSIETGLRKLAEQGVTEVILFPLYPQYAMSTTETVIAKAEEVRKLKFPNLSIKYVGSFYQQELYLDCLAQSIKEKLPEDFDTLLFSYHGVPERHLPKVDKKITSLIPNWGEDQGKPLYEIDYKQQCLNTTVAIASRLNLDGKAQTSFQSRLGKDKWIEPYTDATLQNLPKQGKKKLVICCPAFVSDCLETLEEISVEARSIFLNAGGETFHYISCLNDEDRWIDVIKALVSESTEVGNHQELF
>NZ_CP029149.1|WP_160224143.1|1081940_1082351_+|hypothetical-protein
MKRVIVFCLMILLFISCRSYSEKDLIGVYTPVNYRNTFDTIHLKKNNKYYRTVYNKSKERVIEIRGEWSVREDVIEFKSPYFLNLDRDLVMYPELLQDTESNGLGYIWKKVGVFEFCVGYFGVDLPNQNCYRRLND
>NZ_CP029149.1|WP_160224702.1|1079953_1081750_+|elongation-factor-4
MKNIRNFCIIAHIDHGKSTLADRLLEYTNTVTQRELQAQTLDDMDLEKERGITIKSHAIQMDYEYKGEKYVLNLIDTPGHVDFSYEVSRSIAACEGALLIVDAAQSIQAQTISNLYLALENNLEIIPILNKIDLPSANPEEVTDDIVNLLGCKPEDVLRVSGKTGEGVRELLEQIVERIPAPEGNPEAPLQALIFDSVFNPFRGIEAYFKVVNGSIKKGQKVKFMATDRTYDADEVGTLKLKQVAKQEIKCGDVGYIISGIKDAREVKVGDTITSAENPAPNPIEGFEEVKPMVFAGIYPIESEDFEELRASLEKLRLNDASLVFEAESSAALGFGFRCGFLGMLHMEIVQERLDREFGMNVITTVPNVSYHGYTKKEPDVPILINNPSEMMDPTTMDRVEEPYIKASIITKSDFVGPVMTLCIEKRGEIVNQSYLTSDRVELIFNMPLSEVVFDFYDRLKSISKGYASFDYHPIGFRPSKLVKMDILINGDMVDALSSLIHDTNAYTIGKKMCEKLRELIPRQQFDIAVQAALGTKVIARETIKALRKDVTAKCYGGDISRKRKLLEKQKEGKKKMKQIGRVEVPQSAFMAVLKLND
>NZ_CP029149.1|WP_120489775.1|1090010_1091288_+|glutamyl-tRNA-reductase
MKQNLDIHKTSNFSVLSISYEKADAETRGKFAFFDENVKEFVRRISEKQLGDAFVVSTCNRTEIYTTTLNYIFIVEEYCKLIGVHLLDFMRFATVLNREDALNHLFRVAGGLESQIIGDFEIIGQIKNAYNRFKREKKNSNPYLERAINSAIQISKRIKNETGISNGAASVSYAAVHYILNHQQNVSEKNILLLGVGEIGQNTVDNLIKHIYQPKIKIANRSSEKAEKIAEKYHIPSIPYERLNDELPQTDILIVATGAKTPIINKEHFPNNGKKTLIIDLSIPNNVDKTVLENPNITLIDVDQLSVQIQETMEQRRKEIPKAEQIIKLMMKDFFEWEKTRKMAPKIHHFKAVLKNMERNEMHNIHKKHRYVNIDDMELSEKIIQKITNRFAKYIIDHPWKAEEVSKMMHEILVEQPNKEFNEKH
>NZ_CP029149.1|WP_160224148.1|1091274_1092180_+|hydroxymethylbilane-synthase
MRSIKIGTRHSPLALWQAREVERRLQALNLSTEVFPIISTGDKNLSQPLYSMGITGVFTKDLDLALLNKEIDIAVHSLKDVPTQLPEGIKVLAYLERDFPQDVLVRSTAAKDKPLQDLKIATSSLRRRAFWAKQFPNTSFVDIRGNVNTRLQKIEDGLADATLFSLAGIKRLNLNITYEELPFMISAPSQGVVVVVGRDGDNDELNNRVREINHLNTQYCVEVERDFLQTLEGGCTAPIGAIADIQGSEMVFKGRLCSLDGKKCIEINEKFSFSVNQKYGKILAEQVLRQGGEEIMKSLKL
>NZ_CP029149.1|WP_160224149.1|1092180_1092861_+|uroporphyrinogen-III-synthase
MKKILFTKKIDEQLVSNILGGSFYCEYIEAIRIKNRKVKPFNVRGKSIIFTSVNGVKSFFENGFVLNQDFTNRLCFNRVYAVGIKTKRELRKYGVNTYKVFSYAYVLIDFIINKANEECYIHFCGNLALDLFNNKLPLQNISYRRIVVYDTELLYPEINENYDGIVFFSPSGVRSVLTNNDIGQAKVFAIGRTTEDELKKYNIKNIITNNEANLDGIFHSIKNTEF
>NZ_CP029149.1|WP_120489772.1|1092883_1093909_+|uroporphyrinogen-decarboxylase
MIKNDLYLRALKGETVERPPVWMMRQAGRYLPEFIALRDKYDFFTRCQTPELAAEITVQPIRRFPLDAAILFSDILVVPQAMGIDFKMKEGIGPWLETPIRTQAQVDAIKLPQVDETLGYVFDAIELSLQMLNNDIPLIGFAGSPWTILCYCVEGKGSKAFDIAKSFCFQQPEVAHQLLQKITDTTIAYLKRKVEKGVSAVQIFDSWGGMLSPEDYREFSWKYIHQIVEELSKVTHTVVFAKGCWYALEEMSLSKASALGVDWTVSPELARHFTQNRITLQGNFDPARLHSSPEVIKRMVGEMIHRFGKDKYIANLGHGILPNIPLENAEAFVRAVVDWKP
>NZ_CP029149.1|WP_160224150.1|1093930_1094659_+|tRNA-threonylcarbamoyladenosine-dehydratase
MMANWLERTELLIKKTGVERLQNANILVVGLGGVGGFAAEFIARAGVGKMTIVDGDTVDITNINRQLPALHSTIGKAKTELISQRLLDINPYLQLTALHQFLNPENMEPLLDGQDFDYILDCIDSVSPKIELIKAARKRKIKLVSAMGAGGKTDPSMVMVRDISKTNNCFLAKQIRKRLRKENINKGFRCVFSNEIQAEDSLKMTDGSQFKKSFYGTMSFMPAIFGLYAAAEAINHILKIED
>NZ_CP029149.1|WP_120489770.1|1094655_1095003_+|ribonuclease-P-protein-component
MKKYAYPRSEKLKQDKDFALLFKKGKWRTAGAVRLVFTSSDEVQKPKVGVSASKKLFKRSIDRNRAKRLLRAVYRHHKEAFAQKFGSQTLAMLFWISPELPPNYQTVEADFLKLL
>NZ_CP029149.1|WP_160224151.1|1095054_1095942_-|glycosyltransferase
MDLPLVSIVCNCYNHAPYVLEAIQSVQQQTYKNIELIVLDNGSTDDSLHIIRDYLKDFPEVRFIHLNEPLPLPKAFNTMFKYTNGDFLIDLSADDVLLTDCVQKQIDFFQKQDDSTGIVFGNAYLIDENGQNPTPFFDVDNEGKVLDSRLHSFDYYLMLHSGKTFCSVSAMMRRTHFIALNGYDESLFFEDLDYWYRLSRRFRIRFIDDFLVKKRQLNHSLGAQIDAKGKHTHLLNLSLIKIYRSAISYNSPKENKALLQRIHYSMSVCFQHRLWADLLRFTYLKFLCQVHCLFR
>NZ_CP029149.1|WP_160224152.1|1095963_1097034_+|glycosyltransferase
MNKNYKIAIVIYKFSEGGLERIVSNSTFAFHQMGCEVHLYVLSSQVGYHYAGRLHQYPIDALSGVSKMKAYMRFAKSLKQEDFDFIIDHRCRLNLLMEFFWSKYIYRNQKVFHYIHSADVDSFLFRSERLNRFLYSGSFICVSKALAHSLQKKFPSLDFHTIYNPVGFSKDYSNNRGEYIITLSRMADDNQKQVDVLLSCYAKSLLPSKGIRLMIIGNGSQMQMMKELANELGIQHLVDFKGFIPEPYQYIADAKYTVLSSKYEGLPTVLIESLMLGTPVIAFDCPTGPAEIIINKENGLLIENQNEDEFIKGMNLLAEDHNLYEYLKAHTKESAKIFSVENFISEWKELFKKHKR
>NZ_CP029149.1|WP_160224153.1|1097030_1098110_+|glycosyltransferase-family-4-protein
MRLLYISTGITNSGGVSRVLSLKANAFADALGYEVHIFSTNDDSQTTFFSFSEKVKIHFSKYKNIGLHNIFGFRKEVRELNKALNPDAIFITDNGLKSFLIYDCLYPKAIKMYEIHSSTDAFLNQAYYSGIKNKIYQWLIRHQIKKFDKIIVLKEQFKLGFVPESKQLAIPNPIPFLVDAQSSLHHKKAIAVGLITPRKGYERMLRSWKKVVQKHPDYQLEIYGEATGNYSIMPLISELGLENQVKVFPPVRDIEQRYLEADFLLHSAYSEPFGMVFIEAMALGLPVVCHKTEADDIVINGKNGWVAEDEDDYTQKILQLIEHPEFLHSFSENAVETSKRFQLKEIMHRWQVLLSQRKT
>NZ_CP029149.1|WP_120489767.1|1098193_1098586_+|WxcM-like-domain-containing-protein
MKFRMISLPKIEDPRGNLSVIEKDILPFVFKRVYFLYDVPSGAERGGHAHKEQQEFLIALSGSFDVILNDGKETSTIHLNTPNKGLLIPNGYWRELKHFSSGAVCLVLSSDVYQEEDYIRDYDEFIASRR

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Crispr_ID: NZ_CP029149_7

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP029149_7

1138495-1138607

Orphan

Consensus_repeat	Method
GCGGTTAGTTTGTAGTAAGTGCGCCACCTGCAAGGTGCCACGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP029149_7

>merge|NZ_CP029149|7|1138495-1138607|CRISPRCasFinder
GCGGTTAGTTTGTAGTAAGTGCGCCACCTGCAAGGTGCCACGCCAGTGGGCATCTAGCTATTGGTGGTGCGCGGTTAGTTTGTGGTAAGTGCGCCACCTGCAAGGTGCCACGC

>NZ_CP029149|7|6|1138495-1138607|CRISPRCasFinder
GCGGTTAGTTTGTAGTAAGTGCGCCACCTGCAAGGTGCCACGC	CAGTGGGCATCTAGCTATTGGTGGTGC
GCGGTTAGTTTGTGGTAAGTGCGCCACCTGCAAGGTGCCACGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP029149.1\|WP_160224201.1\|1147892_1148045_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_160224194.1\|1143563_1145297_-\|T9SS-type-A-sorting-domain-containing-protein	unknown	unknown	gnl\|CDD\|275036
NZ_CP029149.1\|WP_160224190.1\|1140054_1141221_-\|glucose-1-phosphate-thymidylyltransferase	unknown	unknown	gnl\|CDD\|274907
NZ_CP029149.1\|WP_160224200.1\|1147016_1147775_-\|triose-phosphate-isomerase	unknown	unknown	gnl\|CDD\|234589
NZ_CP029149.1\|WP_120489640.1\|1132606_1133086_-\|cytidine-deaminase	unknown	unknown	gnl\|CDD\|273572
NZ_CP029149.1\|WP_120489745.1\|1131780_1132515_+\|30S-ribosomal-protein-S2	unknown	unknown	gnl\|CDD\|235396
NZ_CP029149.1\|WP_120489641.1\|1131182_1131569_+\|30S-ribosomal-protein-S9	unknown	unknown	gnl\|CDD\|178888
NZ_CP029149.1\|WP_160224198.1\|1146290_1146992_-\|SIMPL-domain-containing-protein	unknown	unknown	gnl\|CDD\|377344
NZ_CP029149.1\|WP_120489746.1\|1130721_1131177_+\|50S-ribosomal-protein-L13	unknown	unknown	gnl\|CDD\|181703
NZ_CP029149.1\|WP_120489633.1\|1141308_1141560_-\|type-B-50S-ribosomal-protein-L31	unknown	unknown	gnl\|CDD\|234969
NZ_CP029149.1\|WP_160224182.1\|1138629_1140042_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_160224174.1\|1126107_1127511_+\|spore-maturation-protein	unknown	unknown	gnl\|CDD\|225336
NZ_CP029149.1\|WP_120489639.1\|1133172_1134381_-\|3-phosphoshikimate-1-carboxyvinyltransferase	unknown	unknown	gnl\|CDD\|238797
NZ_CP029149.1\|WP_160224179.1\|1135364_1137284_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_160224180.1\|1137353_1138070_+\|DUF4469-domain-containing-protein	unknown	unknown	gnl\|CDD\|373337
NZ_CP029149.1\|WP_160224192.1\|1141797_1143540_-\|T9SS-type-A-sorting-domain-containing-protein	unknown	unknown	gnl\|CDD\|275036
NZ_CP029149.1\|WP_160224175.1\|1127583_1130532_+\|insulinase-family-protein	unknown	unknown	gnl\|CDD\|223685
NZ_CP029149.1\|WP_160224177.1\|1134380_1134710_-\|nucleotide-pyrophosphohydrolase	unknown	unknown	gnl\|CDD\|212138
NZ_CP029149.1\|WP_160224203.1\|1148462_1148936_+\|copper-resistance-protein-NlpE	unknown	unknown	gnl\|CDD\|377235
NZ_CP029149.1\|WP_160224196.1\|1145445_1146273_-\|50S-ribosomal-protein-L11-methyltransferase	unknown	unknown	gnl\|CDD\|234786

Protein	Function_ID	Function_description	E-value
NZ_CP029149.1\|WP_160224194.1\|1143563_1145297_-\|T9SS-type-A-sorting-domain-containing-protein	gnl\|CDD\|275036	TIGR04183, hypothetical_protein, Por secretion system C-terminal sorting domain. Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.	1.07111e-08
NZ_CP029149.1\|WP_160224200.1\|1147016_1147775_-\|triose-phosphate-isomerase	gnl\|CDD\|234589	PRK00042, tpiA, triosephosphate isomerase; Provisional.	3.10032e-134
NZ_CP029149.1\|WP_120489640.1\|1132606_1133086_-\|cytidine-deaminase	gnl\|CDD\|273572	TIGR01354, Cytidine_deaminase, cytidine deaminase, homotetrameric. This small, homotetrameric zinc metalloprotein is found in humans and most bacteria. A related, homodimeric form with a much larger subunit is found in E. coli and in Arabidopsis. Both types may act on deoxycytidine as well as cytidine. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides].	3.24001e-35
NZ_CP029149.1\|WP_120489745.1\|1131780_1132515_+\|30S-ribosomal-protein-S2	gnl\|CDD\|235396	PRK05299, rpsB, 30S ribosomal protein S2; Provisional.	1.25871e-141
NZ_CP029149.1\|WP_120489641.1\|1131182_1131569_+\|30S-ribosomal-protein-S9	gnl\|CDD\|178888	PRK00132, rpsI, 30S ribosomal protein S9; Reviewed.	4.97191e-78
NZ_CP029149.1\|WP_160224198.1\|1146290_1146992_-\|SIMPL-domain-containing-protein	gnl\|CDD\|377344	pfam04402, SIMPL, Protein of unknown function (DUF541). Members of this family have so far been found in bacteria and mouse SwissProt or TrEMBL entries. However possible family members have also been identified in translated rat (Genbank:AW144450) and human (Genbank:AI478629) ESTs. A mouse family member has been named SIMPL (signalling molecule that associates with mouse pelle-like kinase). SIMPL appears to facilitate and/or regulate complex formation between IRAK/mPLK (IL-1 receptor-associated kinase) and IKK (inhibitor of kappa-B kinase) containing complexes, and thus regulate NF-kappa-B activity. Separate experiments demonstrate that a mouse family member (named LaXp180) binds the Listeria monocytogenes surface protein ActA, which is a virulence factor that induces actin polymerization. It may also bind stathmin, a protein involved in signal transduction and in the regulation of microtubule dynamics. In bacteria its function is unknown, but it is thought to be located in the periplasm or outer membrane.	8.25456e-08
NZ_CP029149.1\|WP_120489746.1\|1130721_1131177_+\|50S-ribosomal-protein-L13	gnl\|CDD\|181703	PRK09216, rplM, 50S ribosomal protein L13; Reviewed.	4.09186e-89
NZ_CP029149.1\|WP_120489633.1\|1141308_1141560_-\|type-B-50S-ribosomal-protein-L31	gnl\|CDD\|234969	PRK01678, rpmE2, type B 50S ribosomal protein L31.	2.1143e-45
NZ_CP029149.1\|WP_160224174.1\|1126107_1127511_+\|spore-maturation-protein	gnl\|CDD\|225336	COG2715, SpmA, Uncharacterized membrane protein, required for spore maturation in B.subtilis. [General function prediction only].	1.86373e-67
NZ_CP029149.1\|WP_120489639.1\|1133172_1134381_-\|3-phosphoshikimate-1-carboxyvinyltransferase	gnl\|CDD\|238797	cd01556, EPSP_synthase, EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase (5-enolpyruvylshikimate-3-phosphate synthase) (EC 2.5.1.19) catalyses the reaction between shikimate-3-phosphate (S3P) and phosphoenolpyruvate (PEP) to form 5-enolpyruvylshkimate-3-phosphate (EPSP), an intermediate in the shikimate pathway leading to aromatic amino acid biosynthesis. The reaction is phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate. It is found in bacteria and plants but not animals. The enzyme is the target of the widely used herbicide glyphosate, which has been shown to occupy the active site. In bacteria and plants, it is a single domain protein, while in fungi, the domain is found as part of a multidomain protein with functions that are all part of the shikimate pathway.	3.63136e-99
NZ_CP029149.1\|WP_160224190.1\|1140054_1141221_-\|glucose-1-phosphate-thymidylyltransferase	gnl\|CDD\|274907	TIGR03991, alt_bact_glmU, UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase. The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Homologs of this enzyme are identified in a number of bacterial organisms and modeled here. A number of these are observed in proximity to the GlmS and GlmM genes, and phylogenetic profiling by PPP identifies the LEPBI_I0518 gene in Leptospira biflexa as a likely Glm-system candidate. Multiple sequence alignments of these bacterial homologs with their archaeal counterparts reveals significant structural differences, necessitating the construction of separate models. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars].	2.18516e-142
NZ_CP029149.1\|WP_160224180.1\|1137353_1138070_+\|DUF4469-domain-containing-protein	gnl\|CDD\|373337	pfam14848, HU-DNA_bdg, DNA-binding domain.	1.4305e-38
NZ_CP029149.1\|WP_160224192.1\|1141797_1143540_-\|T9SS-type-A-sorting-domain-containing-protein	gnl\|CDD\|275036	TIGR04183, hypothetical_protein, Por secretion system C-terminal sorting domain. Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.	9.09419e-09
NZ_CP029149.1\|WP_160224175.1\|1127583_1130532_+\|insulinase-family-protein	gnl\|CDD\|223685	COG0612, PqqL, Predicted Zn-dependent peptidases [General function prediction only].	1.68861e-51
NZ_CP029149.1\|WP_160224177.1\|1134380_1134710_-\|nucleotide-pyrophosphohydrolase	gnl\|CDD\|212138	cd11531, NTP-PPase_BsYpjD, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain putative pyrophosphatase YpjD from Bacillus subtilis and its bacterial homologs. This family includes a putative pyrophosphatase Ypjd from Bacillus subtilis (BsYpjD) and its homologs. Although its biological role has not been described in detail, BsYpjD shows significant sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, BsYpjD contains a single MazG-like domain.	1.4658e-41
NZ_CP029149.1\|WP_160224203.1\|1148462_1148936_+\|copper-resistance-protein-NlpE	gnl\|CDD\|377235	pfam04170, NlpE, NlpE N-terminal domain. This family represents a bacterial outer membrane lipoprotein that is necessary for signalling by the Cpx pathway. This pathway responds to cell envelope disturbances and increases the expression of periplasmic protein folding and degradation factors. While the molecular function of the NlpE protein is unknown, it may be involved in detecting bacterial adhesion to abiotic surfaces. In Escherichia coli and Salmonella typhi, NlpE is also known to confer copper tolerance in copper-sensitive strains of Escherichia coli, and may be involved in copper efflux and delivery of copper to copper-dependent enzymes.	1.5151e-27
NZ_CP029149.1\|WP_160224196.1\|1145445_1146273_-\|50S-ribosomal-protein-L11-methyltransferase	gnl\|CDD\|234786	PRK00517, prmA, 50S ribosomal protein L11 methyltransferase.	8.59852e-91

>NZ_CP029149.1|WP_160224180.1|1137353_1138070_+|DUF4469-domain-containing-protein
MKNTLKAWLRDNPLTSDPSDFVGVPASVGSVSIAEIVAELKKEGMEIKEETAIDIVSRFNRKSTELVLQGYVVNTGLVIMRPAIKGAFRDRTWDKDKHSVYVNVNQGVELRKAISQTKVEFLGEQSSPMAIFGITDLSTGKTDGTLTKGKNAEIKGSYLKVAGTHADNGIYLTNIDTKAKTKLEDIVINEPSRLLVLIPASLPAGNYELSITTQFSNTSKVFLKTPRTEVLNTPVVIA
>NZ_CP029149.1|WP_160224179.1|1135364_1137284_+|hypothetical-protein
MRFKMILAFVLIGVLASAQTEYDGRVGINTETPKATLDISRNTSVSSSSVQGVIFPRVTSVERDAFNSADIVEGTMIYNTDRKCVEIFSNSGWDCISSVAPSLPPGVTLQIMGAGWDGVFQAGTAVAAGSGTHKVKLLINNTGATPYTQNLSSAMTITNIPGTLPGGVPAPTGTVALDGAQNSSVTVAPGTSQIISYNLKGMPQVGNIKATFRIGIYNVEQTYTVSQGTALFQDHSIFVFSWKEDSSVQGTPPITSSYQGKIDGSIYKIPVKIPYKNGDGKSFGEFTKTVSIGTAPNQKTLKLTIPAGRLHQSPSTGLYNVITGTLEVIDGTYNAPLLESGSADELIATIPVQLTSAMTPFNLKVYATGGVKDKQYNHETAGVAGRYDHRFVYSKIMTYDGQIWLDKNLGAYFADANRIADFGYDQIYEMRVPNTLMDYRMFGSAFQWGRVADGHELIDWPSSLSGPSPSGPNGVYRYNSVTDFPLGTTTDAWKRYNKTEYNANVSSYTDPCPSGWHTPTQPEMHQLKLNTVGGGILVDIKSYRGSFFTEILRLGTASGTSPFSIEQWSFLWTKTQDTSNDAYYIRASSYEDRNPQFRVPQALDPSVSPGGETVGQILGVGNNITIQKISTMSVRCIKD
>NZ_CP029149.1|WP_160224177.1|1134380_1134710_-|nucleotide-pyrophosphohydrolase
MEISSLQKKVDEWIKTVGVRYFNELTNMAILTEEVGEVARIIARRYGEQSEKETDKTKDLGEELADVLFVLLCLANQTDTDLQKAFDKKMISKTKRDRDRHKNNPKLKD
>NZ_CP029149.1|WP_120489639.1|1133172_1134381_-|3-phosphoshikimate-1-carboxyvinyltransferase
MKIHKPKLPKEIQIKGSKSETNRLLILQKVLGAIEILNPSSSQDTELLKSALASQNKIIDVHNAGTAMRFLTSFFAIQEGRETLLTGSERMKQRPISPLVEALQELGADIQYLERAGFPPLKIKGKKIEKSSVRIPAGISSQFITSLILIGGSLASGLMIELVGEITSRPYLEMTLKILKTLYPNAPISFQGQKIFIPYLLNAKPSQSSFIVESDWSSASYFYSFAAIGRREIKLSNFKRDSLQGDAVVSKIYRNFFGVETVFNDNEHSLSLIPKADFSRPTEIHLDMNDCPDIAQTVCVTAAAMQIPFTIEGLATLKIKETDRLLALHNELKKLGCHTETSHCSIKTLHYTKPELPISIKTYDDHRMAMSFAPYSLLQEIEIQNPEVVEKSYPEFWKDLGI
>NZ_CP029149.1|WP_120489640.1|1132606_1133086_-|cytidine-deaminase
MEKEFIIKYELINGKDELSEADRKLYDAAAKVRETAYAPYSDFLVGCALLLESGEIITGSNQENAAYPSGLCAERTTIFWTSANHPDAKIKKIFVIGGPRTKPDAPATPPCGACRQSMLEYESKQNEEIEFFFSSLEGAIYKTKSIRDLLPFSFDLSFL
>NZ_CP029149.1|WP_120489745.1|1131780_1132515_+|30S-ribosomal-protein-S2
MAKVNVKDLLEAGVHFGHMTRKWNPNMAPYIFMEKNGIHIIDLHKTAVKLEEACTALEKLTSAGKKVLFVATKKQAKEVVAKHAQELNMPYITERWPGGMLTNFVTIRKAVKKMNAIDKMKKDGTFETLSKKERLQVDRQRANLEKNLGSIADMVRLPSAVFVVDILREHIAVTEAKKLGIPVFGIVDTNSDPRKVDFVIPGNDDASKSVDMILSIVADAVKEGLSQRKTEKSKEEGKETADAE
>NZ_CP029149.1|WP_120489641.1|1131182_1131569_+|30S-ribosomal-protein-S9
MSTVHKIGRRKTSVARVYLKPGTGNIKVNGKDAKEYFSTDVLVYKLNQPFALTETVEQYDVTVNVFGGGITGQAEAIRLGISRALCEVNAEYRLALKPAGLLTRDARMVERKKPGQKKARKRFQFSKR
>NZ_CP029149.1|WP_120489746.1|1130721_1131177_+|50S-ribosomal-protein-L13
MNTLSYKTVSANKATAKKEWVVVDAEGQPLGRLASVVAKILRGKHKTNFTPHVDCGDNVIVLNAGKVSLSGNKWADKTYIWHTGYPGGQKSVTATELVKKHPLRLVEKSVKGMLPKNKLGTQLYKNLYVYEGAEHKHEAQQPKVININEFK
>NZ_CP029149.1|WP_160224175.1|1127583_1130532_+|insulinase-family-protein
MIKRSLSTLFLAAVLSFNAYGQSYQWKEAQSGGYTYKYVTNDPTNARFYTLKNGLTVILSPTNKEPRIQCYVAVKAGSKTDPKTNTGLAHYLEHMLFKGTDKYGSLDWKKEKKELDKIDALYEKYNKTKDEKKRKEIYKQIDSVSGVASKYAIANEYDKMMSAMGAQNTNAFTSFEKTVYTDDIPAGSLDKYLAVQSERFRNPILRIFHTELEAVYEEKNRSLDSDGSLVFETLFENLFKKHNYGLQTTIGTVEHLKNPSLVEIRKYFHKYYVPNNMAIVLSGDFNPDEVIKKIDKDFSYMKAKKVPKYTFEQETPITSPVVKEIVGPDAESVTIGFRLPGNKDKDVILANLVGDILTNGKAGLLDLNLVKKQKLLRAGAFTFTLIDHGVLYLSGAPTKGQSLQEVKDLILSEIENLKKGNFDDDLIPSIANNMKKDIIQETESYNTRANILMQAFTDEQDWKDRVAYLDDLSKVKKSDVVAFANKYLGDNYVAILKKKGARTDLQKIEKPTITPVETNADKQSDFVKAVEKIPSIPSQPVFLDYDKDLQKSKLGDAEVLYVQNKENQLFRLRYRYKISKFNDLKVPLATQYLHYLGTDKKSAEEISKEFYKIASSFSISSGEEYTTVTIEGLQENFDKAVKLYEDLVANAQPNEEALKALKARLHKSRTDAKANKSTIMGALTNYALYGAKNKFNHTFTNAQLDALTSKDLKSSLCSLRDAEQTIIYYGPASLKEVEDKLAKEHHIFGYNSPKGYKKCTVPQAVTFTQTEQKENRVLFTNYEMVQAETRWLRNTTPYNPQETTLVRVFNNYFGNGMGSIVFQTIRESKALAYSTYGVYVSPSKKNDKYYMQAYVGSQADKFKEAVSAMNDLLNTLPVLSGSLDLAKNQVKKDIQTERITQDGIIYNYLAAQNLGLKEDIRKQVYQNVDKITMRDVQSFHEKYFSQKPYTYVVLASDKKVSKEELQKIGKVQTLSLEELFGY
>NZ_CP029149.1|WP_160224174.1|1126107_1127511_+|spore-maturation-protein
MVLSRIWSAFIIIAVVVASFKYMLSGNYQTIYNDMVVGKSGDTVQIAQKLVVDLPFDAKEKFKESHNFSDGKIHYRYNPTDETVKIYRIQETDGVIGTSQTAVNICIGLIGIMTLFMGFMSIAEKAGGINLLSRLIQPFFSRLFPEVPKNHPAFGHMLMNFSANLLGLDNAATPFGLKAMESLQSINPNKDKASNSQIMFLCLHAGGMTLIPVSIIAIRASMGSVTPTDIFLPCMIATFSATLAAMIIVSLYQRLNLLQPVVLAYIGGISVIIALLVMYLVHLSKDELDTFSKVLSNGLILLIFLAIVLGGIYKRINIFDAFIEGAKEGFTTCVKIIPYLVGMLIAISMLRTSGVFDVVIEGMKWLAGVANLDARFVDGLPTALIKPLSGSGARGMMIDTMSAFGADSFQGRLSAVLQGSSDTTFYVIAVYFGAIGIKNTRYTVTAMLLADLVGIITSVVLAYLFFS
>NZ_CP029149.1|WP_160224182.1|1138629_1140042_-|hypothetical-protein
MKIKSLFSLSFFALILIISCKRDEINFETPNAELKFSRDTVFCDTIYNQVRSETYAVKVFNTENRDIFIPKISLQGGNTSPYRINVDGKAGVEFRDVPLRKHDSLYIFVEIAPVANSKEAIAEDRIIFSMPKGEQHITLFSVVQDAEFFIQTQTNPNLLSEDTNWTSDKAKIIFGELTLAEGKTLSVAEGTKIYFTKGSGLKISKNAKLNLNGALDNEILLRGDRNDTRYDTIPLNWKGIRLEEGASLNANYAKIFGGETGIQLYKASATLRNTIMHSFQDYGIRSINSQLQAENLVMNSCGGANLALLGGGEASLTHCTLANEWKQNYSLPAYGVYATNEWTNDSGNKEINNLNLKIQNSILYGSAETSIFFEPVQGYDFNYLISHSLVKYSNKSGFNFDSNALIVQSIKNEDPKFARPYITKMNLRLKPNSPAIGKGSTTVAASVSKDIKGEDRTSSPNLGAYQTPTR
>NZ_CP029149.1|WP_160224190.1|1140054_1141221_-|glucose-1-phosphate-thymidylyltransferase
MQLVFSDAQYWEDFLPLTFTRPVAEMRCGILTFAERWIKLLNISEKAYITEEYLEGKYPHPKEVESLFIVPNFLPTLKVVEQIKELKSGEALVYENELLAARINMKNFSLSQIKKMTDIEGELIFFKQPTDLFSLNDKAINFDFELLTKGRKSQPLSETNGLLGNASDLFIEEEAVVEFSTLNTKTGKIYIGKDAEIMEGCHLRGPIALCEGAKFNLGAKIYGATTIGPHSKVGGEVNNIIIFGYSNKGHDGFVGNSIIGEWCNLGADTNSSNLKNNYANVKLWNYRQKKFIDTGLQFAGLIMGDHSKTAINTQLNTGTVVGVAANIFKTGFPPNLVSNFSWGGMKADARFNLEKACEVAEKVMSRRKVSLTDADKDILKYIYEHFTD
>NZ_CP029149.1|WP_120489633.1|1141308_1141560_-|type-B-50S-ribosomal-protein-L31
MKKGIHPENYRLVVFKDMSNDEMFLCKSTAETKDTIEYEGQEYPLVKMEISSTSHPFYTGKVKLVDTAGRVDKFMNKYKKFAK
>NZ_CP029149.1|WP_160224192.1|1141797_1143540_-|T9SS-type-A-sorting-domain-containing-protein
MKKICIPLTIAALAFANAQQKFEEVTPTSFKAFYYGKASIGDVNNDGFKDVFFTGTVDEDGDNYPDITKNELYKNDNGTFVPLQLFPENAVHFSDNKFIDFDNDGLLDLVTTGLSYNDVVNYRTYRWKNTGTKFELQDNLDGRTFGNIEVFDLNHDGLLDYAVNGLRFIENVGFEYKTDVYLNSKTGFLDKRKDIIPEGRQYGKLRVFDIDNDGYLDAVLFGLNENTEEKFTIYKNNKGTFEISQELDGFQNGDLNYADFDSDGDLDFVISSLDKEGKHHLIYFKNNGGIFTPHQEINSDHLNDSSIDIGDINGDGYYDFIAIGSGKNSANNVTSVFIYNPTTDNFEEQYFDIDPVGGNGGINLFDFNNDNNLDVLLYGFDWKISGYPYVTKLFKNVQSITNKAPEPPTYLSATVSADKVTFEWSSGNDDKTPSKALQYEFIVGSAPGKSDIAKYTVTTPHWFLQKENLPNTIYWRVKSIDASKVLSNDSEEQVVSNLSVNNITKESGAVLYPNPVKDVLNIRTEAKVKSYRIINTSGQVVLSKTTDKKSINLSGLSKGLYIVEITFEDAKPLSAKIIVN
>NZ_CP029149.1|WP_160224194.1|1143563_1145297_-|T9SS-type-A-sorting-domain-containing-protein
MRKVYLPLCLSVFACINAQQFKEVMPPAFKNFFFGRAAIADFNNDGYKDLFFTGTVDENNNNLPDYSFNTFYKNTNGTFSPLQSFRENSAYLGDAKFIDFDNDGLLDLVATGLSSDEHRTLRWKNTGDAFVLDNISDGRIRGNIESFDLNHDGLLDYAVNGFQYKDIGGVNYKTDLYINSKSGFSDANNETIPLGSLNGKLRIFDINNNGLHDAVIFGTTASGTSEKTFTVYKNDNGVFNTHQQLEGLVNGDLAYADFNADGYLDMIACGKDKNNNYHLIYYKNDGAGKFLKKEISTEYLDNSSLDVGDINDDGYYDFIVIGSGSSASNTTKVFVYNSSSDTFEYTDYGIPQLGGNGGINLFDFNNDNKLDILMYGANNKETDKPHKTKLLENTQDITNNAPNPPANLSSSLSDNKILFEWNGANDDKTPSKALQYEFIVGSAPGKSDIAKYTVTTPHWFLQKENLPNTIYWRVKSIDASKVLSNDSEEQVVSNLSVNNITKESGAVLYPNPVKDVLNIRTEAKVKSYRIINTSGQVVLSKTTDEKAINLSGLSKGLYIIEIAFEDAKTLSAKIIIN
>NZ_CP029149.1|WP_160224196.1|1145445_1146273_-|50S-ribosomal-protein-L11-methyltransferase
MTEYLEFSFKIAPLQPWSEILMAELIEIGFDSFTEELDGILGYIPEESFNENSLKSLPLMSAPEVKISYTYQQMPNINWNEEWEKNFSPINIEEKVLIRAEFHEPRPDLHEIIIQPKMSFGTGHHPTTHLMIQQMLDMDFTDKKVLDMGCGTSVLAIYAKQRGANEVTAIDIDEWSVENSIENAERNSVQLNISQGTAESLGAESYDIILANINRNILISDIPTYVSVLKDKGQLLLSGLCFFDVEDILQVCNEQGLKLTHQQQREEWCSLLLEK
>NZ_CP029149.1|WP_160224198.1|1146290_1146992_-|SIMPL-domain-containing-protein
MKKLILLGALVAAHALAFAQKNFIDQPFVEVSAKADSLVVPDRIYLSIRIEEASSKNRKSVEEQEKQMLSALRRAGINTDKDLEMEDLSSSLRTFFLKGKNIIKEKNFNLLVRDANTAARVLLSLEEEDISNINISKIEYSKTEELLLSLKAQAMQKSKYLAQKLAQSVGQKAGKAIFMSDNAKQSPSYGIAGSSTGIMVRGISSMSLKSAPIDVEFKKIKLEAEVSAMYILE
>NZ_CP029149.1|WP_160224200.1|1147016_1147775_-|triose-phosphate-isomerase
MRKNIVAGNWKMNKNFQEAESLMKELADYKKNHKTQCEVYIAPPSLYLTTAKTIFANNEVEVYSQDVSEHASGAYTGEISTDMLQSVGVNGSLVAHSERRQYHGETDISAGKKVKALLDAGLTPVYCNGETLDQRKAGKHLDIVKEQTETALFGLSAEEIQKVVIAYEPVWAIGTGETATPEQAQEIHAHIRNLIAEKYGKAVADEISILYGGSVKPENAKEIFSQPDIDGGLIGGAALKIEDFSKIIEAFN
>NZ_CP029149.1|WP_160224201.1|1147892_1148045_+|hypothetical-protein
MIELLRLYIAILFGQLEKRDDLARPSEGVSLSRAKVSRPPERYSLAKPAY
>NZ_CP029149.1|WP_160224203.1|1148462_1148936_+|copper-resistance-protein-NlpE
MKKMMLPLLCAGLLLAACKKSEPESVETPVEDSASASDELPADAIPVASEELGAIAGTYAGVLPCADCEGIEETLTLNADGSYVRESKYQGEKAKDATPDKLEGKFSYDSATKRVTLEGVKEGSSLYEVDGDKLYFLDTDGKRVEGELASNYILTKK

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Crispr_ID: NZ_CP029149_8

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP029149_8

1328989-1329081

Orphan

Consensus_repeat	Method
AGTAACGCTATCAGGGATTTTTAT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP029149_8

>merge|NZ_CP029149|8|1328989-1329081|CRISPRCasFinder
AGTAACGCTATCAGGGATTTTTATGGCTTTAAGATTATTGCAGCCATTGAACGCAGAGTCTTCAATCTCAGTAACGCTATCAGGGATTTCTAT

>NZ_CP029149|8|7|1328989-1329081|CRISPRCasFinder
AGTAACGCTATCAGGGATTTTTAT	GGCTTTAAGATTATTGCAGCCATTGAACGCAGAGTCTTCAATCTC
AGTAACGCTATCAGGGATTTCTAT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP029149.1\|WP_160224304.1\|1324650_1326279_-\|chaperonin-GroEL	unknown	unknown	gnl\|CDD\|234573
NZ_CP029149.1\|WP_120489493.1\|1330502_1332617_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|238657
NZ_CP029149.1\|WP_160224303.1\|1323463_1324591_-\|DUF3800-domain-containing-protein	unknown	unknown	gnl\|CDD\|378919
NZ_CP029149.1\|WP_160224313.1\|1335084_1336143_-\|DoxX-family-protein	unknown	unknown	gnl\|CDD\|225168
NZ_CP029149.1\|WP_160224312.1\|1334726_1335080_-\|TerB-family-tellurite-resistance-protein	unknown	unknown	gnl\|CDD\|143581
NZ_CP029149.1\|WP_160224314.1\|1336146_1336695_-\|DUF1599-domain-containing-protein	unknown	unknown	gnl\|CDD\|377892
NZ_CP029149.1\|WP_160224300.1\|1319507_1319669_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_160224305.1\|1326298_1326577_-\|co-chaperone-GroES	unknown	unknown	gnl\|CDD\|178988
NZ_CP029149.1\|WP_160224308.1\|1327512_1328304_-\|NAD(+)-synthase	unknown	unknown	gnl\|CDD\|238309
NZ_CP029149.1\|WP_120489486.1\|1338220_1339465_-\|GTP-binding-protein	unknown	unknown	gnl\|CDD\|180120
NZ_CP029149.1\|WP_160224310.1\|1332630_1333788_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379448
NZ_CP029149.1\|WP_160224316.1\|1339526_1340435_-\|sulfate-adenylyltransferase-subunit-CysD	unknown	unknown	gnl\|CDD\|235375
NZ_CP029149.1\|WP_160224302.1\|1321240_1323073_+\|lysophospholipid-acyltransferase-family-protein	unknown	unknown	gnl\|CDD\|153248
NZ_CP029149.1\|WP_160224307.1\|1327225_1327504_-\|barnase-inhibitor	unknown	unknown	gnl\|CDD\|225346
NZ_CP029149.1\|WP_120489484.1\|1340499_1341195_-\|phosphoadenylyl-sulfate-reductase	unknown	unknown	gnl\|CDD\|234997
NZ_CP029149.1\|WP_160224299.1\|1319088_1319490_-\|type-II-toxin-antitoxin-system-VapC-family-toxin	unknown	unknown	gnl\|CDD\|350220
NZ_CP029149.1\|WP_160224301.1\|1319979_1321218_+\|aspartate-kinase	unknown	unknown	gnl\|CDD\|239776
NZ_CP029149.1\|WP_160224315.1\|1336756_1338103_-\|sulfite-exporter-TauE/SafE-family-protein	unknown	unknown	gnl\|CDD\|376667
NZ_CP029149.1\|WP_160224311.1\|1333864_1334503_+\|rhodanese	unknown	unknown	gnl\|CDD\|238089
NZ_CP029149.1\|WP_160224306.1\|1326631_1327105_-\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP029149.1\|WP_160224304.1\|1324650_1326279_-\|chaperonin-GroEL	gnl\|CDD\|234573	PRK00013, groEL, chaperonin GroEL; Reviewed.	0
NZ_CP029149.1\|WP_120489493.1\|1330502_1332617_+\|TonB-dependent-receptor	gnl\|CDD\|238657	cd01347, ligand_gated_channel, TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.	2.38582e-40
NZ_CP029149.1\|WP_160224303.1\|1323463_1324591_-\|DUF3800-domain-containing-protein	gnl\|CDD\|378919	pfam12686, DUF3800, Protein of unknown function (DUF3800). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria, archaea, eukaryotes and viruses. Proteins in this family are typically between 215 and 302 amino acids in length. There is a DE motif at the N-terminus and a QXXD motif at the C-terminus that may be functionally important.	0.000883933
NZ_CP029149.1\|WP_160224313.1\|1335084_1336143_-\|DoxX-family-protein	gnl\|CDD\|225168	COG2259, COG2259, Predicted membrane protein [Function unknown].	8.50858e-07
NZ_CP029149.1\|WP_160224312.1\|1334726_1335080_-\|TerB-family-tellurite-resistance-protein	gnl\|CDD\|143581	cd07177, terB_like, tellurium resistance terB-like protein. This family consists of tellurium resistance terB proteins, N-terminal domain of heat shock DnaJ-like proteins, N-terminal domain of Mo-dependent nitrogenase-like proteins, C-terminal domain of ABC transporter ATP-binding proteins, C-terminal domain of serine/threonine protein kinase, and many hypothetical bacterial proteins. The function of this family is unknown.	0.000652865
NZ_CP029149.1\|WP_160224305.1\|1326298_1326577_-\|co-chaperone-GroES	gnl\|CDD\|178988	PRK00364, groES, co-chaperonin GroES; Reviewed.	2.46548e-47
NZ_CP029149.1\|WP_160224308.1\|1327512_1328304_-\|NAD(+)-synthase	gnl\|CDD\|238309	cd00553, NAD_synthase, NAD+ synthase is a homodimer, which catalyzes the final step in de novo nicotinamide adenine dinucleotide (NAD+) biosynthesis, an amide transfer from either ammonia or glutamine to nicotinic acid adenine dinucleotide (NaAD). The conversion of NaAD to NAD+ occurs via an NAD-adenylate intermediate and requires ATP and Mg2+. The intemediate is subsequently cleaved into NAD+ and AMP. In many prokaryotes, such as E. coli , NAD synthetase consists of a single domain and is strictly ammonia dependent. In contrast, eukaryotes and other prokaryotes have an additional N-terminal amidohydrolase domain that prefer glutamine, Interestingly, NAD+ synthases in these prokaryotes, can also utilize ammonia as an amide source .	4.66653e-77
NZ_CP029149.1\|WP_120489486.1\|1338220_1339465_-\|GTP-binding-protein	gnl\|CDD\|180120	PRK05506, PRK05506, bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional.	0
NZ_CP029149.1\|WP_160224310.1\|1332630_1333788_+\|hypothetical-protein	gnl\|CDD\|379448	pfam14064, HmuY, HmuY protein. HmuY is a novel heme-binding protein that recruits heme from host carriers and delivers it to its cognate outer-membrane transporter, the TonB-dependent receptor HmuR. This family of proteins is found in bacteria. Proteins in this family are typically between 214 and 278 amino acids in length.	6.38526e-12
NZ_CP029149.1\|WP_160224316.1\|1339526_1340435_-\|sulfate-adenylyltransferase-subunit-CysD	gnl\|CDD\|235375	PRK05253, PRK05253, sulfate adenylyltransferase subunit CysD.	0
NZ_CP029149.1\|WP_160224302.1\|1321240_1323073_+\|lysophospholipid-acyltransferase-family-protein	gnl\|CDD\|153248	cd07986, LPLAT_ACT14924-like, Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ACT14924. Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are uncharacterized phospholipid/glycerol acyltransferases such as the Pectobacterium carotovorum subsp. carotovorum PC1 locus ACT14924 putative acyltransferase, and similar proteins.	3.53251e-81
NZ_CP029149.1\|WP_160224307.1\|1327225_1327504_-\|barnase-inhibitor	gnl\|CDD\|225346	COG2732, COG2732, Barstar, RNAse (barnase) inhibitor [Transcription].	4.27218e-09
NZ_CP029149.1\|WP_120489484.1\|1340499_1341195_-\|phosphoadenylyl-sulfate-reductase	gnl\|CDD\|234997	PRK02090, PRK02090, phosphoadenylyl-sulfate reductase.	6.76366e-92
NZ_CP029149.1\|WP_160224299.1\|1319088_1319490_-\|type-II-toxin-antitoxin-system-VapC-family-toxin	gnl\|CDD\|350220	cd09872, PIN_Sll0205-like, VapC-like PIN domain of Sll0205 protein and homologs. Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of the Synechocystis sp. (strain PCC 6803) Sll0205 protein and other uncharacterized homologs are included in this subfamily. They are similar to the PIN domains of the Mycobacterium tuberculosis VapC and Neisseria gonorrhoeae FitB toxins of the prokaryotic toxin/antitoxin operons, VapBC and FitAB, respectively, which are believed to be involved in growth inhibition by regulating translation. These toxins are nearly always co-expressed with an antitoxin, a cognate protein inhibitor, forming an inert protein complex. Disassociation of the protein complex activates the ribonuclease activity of the toxin by an, as yet undefined mechanism. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons.	3.42409e-26
NZ_CP029149.1\|WP_160224301.1\|1319979_1321218_+\|aspartate-kinase	gnl\|CDD\|239776	cd04243, AAK_AK-HSDH-like, AAK_AK-HSDH-like: Amino Acid Kinase Superfamily (AAK), AK-HSDH-like; this family includes the N-terminal catalytic domain of aspartokinase (AK) of the bifunctional enzyme AK- homoserine dehydrogenase (HSDH). These aspartokinases are found in such bacteria as E. coli (AKI-HSDHI, ThrA and AKII-HSDHII, MetL) and in higher plants (Z. mays AK-HSDH). AK and HSDH are the first and third enzymes in the biosynthetic pathway of the aspartate family of amino acids. AK catalyzes the phosphorylation of Asp to P-aspartyl phosphate. HSDH catalyzes the NADPH-dependent conversion of Asp 3-semialdehyde to homoserine. ThrA and MetL are involved in threonine and methionine biosynthesis, respectively. In E. coli, ThrA is subject to allosteric regulation by the end product L-threonine and the native enzyme is reported to be tetrameric. As with bacteria, plant AK and HSDH are feedback inhibited by pathway end products. Maize AK-HSDH is a Thr-sensitive 180-kD enzyme. Arabidopsis AK-HSDH is an alanine-activated, threonine-sensitive enzyme whose ACT domains, located C-terminal to the AK catalytic domain, were shown to be involved in allosteric activation. Also included in this CD is the catalytic domain of the aspartokinase (AK) of the lysine-sensitive aspartokinase isoenzyme AKIII, a monofunctional class enzyme (LysC) found in some bacteria such as E. coli. In E. coli, LysC is reported to be a homodimer of 50 kD subunits. Also included in this CD is the catalytic domain of aspartokinase (AK) of the bifunctional enzyme AK - DAP decarboxylase (DapDC) found in some bacteria. DapDC, which is the lysA gene product, catalyzes the decarboxylation of DAP to lysine.	3.30818e-104
NZ_CP029149.1\|WP_160224315.1\|1336756_1338103_-\|sulfite-exporter-TauE/SafE-family-protein	gnl\|CDD\|376667	pfam01925, TauE, Sulfite exporter TauE/SafE. This is a family of integral membrane proteins where the alignment appears to contain two duplicated modules of three transmembrane helices. The proteins are involved in the transport of anions across the cytoplasmic membrane during taurine metabolism as an exporter of sulfoacetate. This family used to be known as DUF81.	2.76993e-33
NZ_CP029149.1\|WP_160224311.1\|1333864_1334503_+\|rhodanese	gnl\|CDD\|238089	cd00158, RHOD, Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.	2.84068e-25
NZ_CP029149.1\|WP_160224314.1\|1336146_1336695_-\|DUF1599-domain-containing-protein	gnl\|CDD\|377892	pfam07659, DUF1599, Domain of Unknown Function (DUF1599).	4.13647e-30

>NZ_CP029149.1|WP_160224308.1|1327512_1328304_-|NAD(+)-synthase
MQTDKVIHHIVGWLKNYAETANAKGYIIGVSGGVDSGVVSTLCAMTGLDTLVLEMPIRQKADQIDRAQEHIAFLERKFKNVKGLRVDLSPTFEEIFTTFKEIGEASEQENLAFANTRSRLRMLTLYHFAQINGLLVCGTGNKIEDFGIGFFTKYGDGGVDISPIADLYKTEVYELAKALDLPESIKNAIPTDGLWDTDRTDEQQIGATYPELEKIQKEYSTKTEQDYTGRALEVYKIFRRMHSAAKHKIEPIPVCYIPEELKK
>NZ_CP029149.1|WP_160224307.1|1327225_1327504_-|barnase-inhibitor
MNLYIDFVDIGDSEDFYTQLKEKLNLPESFNHSPEALLDYISTEVEHPLHIEFINMSVEQLDTFEDLLTALEDTEEEVEGFSFSYYLEQYED
>NZ_CP029149.1|WP_160224306.1|1326631_1327105_-|hypothetical-protein
MKNIIIICALLLSGISIAQTKTYKGAWFEIKYPASFKAKGSIKSATSGSGFDSAVFDSPDGKVQFYIFSPQWSGTAHDIEIKSSEKLVSSETKESGDKELLWWTISAKNNSYTRSYQETKEHSTNWIFGIKYKDDASLKKYKKQYLNFKKSLVQFAD
>NZ_CP029149.1|WP_160224305.1|1326298_1326577_-|co-chaperone-GroES
MSVNFRPLADRVLVEPAPAETKTASGLIIPDTAKEKPQEGTVVAVGDGKKDEPLTVKVGDKVLYGKYAGQELKLDGKDYLIVRESDLLGIIG
>NZ_CP029149.1|WP_160224304.1|1324650_1326279_-|chaperonin-GroEL
MAKEIKFDIESRDALKRGVDALANAVKVTLGPKGRNVVIEKSFGAPHVTKDGVSVAKEIELEDKVENLGAQMVKEVASKTNDIAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVATVVENLKSQSQQVGDNNDKIKQVASVSANNDDTIGGLIAEAFAKVGKEGVITVEEAKGIDTTVDVVEGMQFDRGYQSPYFVTNPDKMVAELDNPYILLVEKKISSMKELLPVLEPVAQQGKALLIISEEVEGEALATLVVNKLRGSLKIAAVKAPGFGDRRKAMLEDIAILTGGQVISEERGFTMENASIELLGRAEKVVIDKDNTTIVNGAGDDTQIKARVNQIKAQIETTTSDYDKEKLQERLAKLAGGVAVLYVGAASEVEMKEKKDRVDDALHATRAAVEEGIVAGGGVALVRAVASLDNVSGSNQDESTGIKIVKRAIEEPLRQIVANAGGEGSVIVAKVAEGKGDFGYNAKTDEFVNMLEAGIIDPTKVTRVALENAASVAGMLLTTECVITEIPKAEPAMPPMGGGMPGMM
>NZ_CP029149.1|WP_160224303.1|1323463_1324591_-|DUF3800-domain-containing-protein
MTIGYADEFGNNSFDFDKQGTHFIVASILIDEKNISTIEQKLKNIRQKYFQTGEIKSSKVANNHKRRIKILTDLQQLDFTIFAVIVDKKSLYSKGFHYKKSFYKYINHLLYKELFNTFDSLSLYVDEFGSNKFMQEFKKYVNKKHPLTLFSNIEFAHQNSKNSIFIQLSDFIAGSLGYIYDETKKNNKSIDIKKLLYNKIAYIRQFPNPLPIIKSISQDDNFDEDISKLSLLRIESFIEKNESNQDPQIKEQIHFLNILLFLQQVKPWVSTKEILNHLNIKRKEPMNKEYFRSKIIGNLRDKGIIIASSQKGYKIPISLKDIGHFIKHGNRVILPMLNRIKEVNNAIKLISKNKINILYNYNELNKIINSIEEIS
>NZ_CP029149.1|WP_160224302.1|1321240_1323073_+|lysophospholipid-acyltransferase-family-protein
MSLISTQELIKATGLTKFGILKNPIAKILMSTTQLTKVNALYDRIKMYKGKAFFDAFIRERGLKYIVFEEDLAKIPKTGAFIIVSNHPLGAIDGILMCKIISDIRPDFKIMGNFLLEKIEPMKEFVIPVNPFGGERKSIRSSATGMRETLKHLEAGGCVGMFPAGEVSNKNNSYNEVRDKEWEKPALKLIKSAKVPVVPMYFNAKNSNFFYSVAKIHPDLQTLMLPSEMMRDRDCPIRVRIGRPISAKVIDEQESTDELSEHLQKKIYLLKSYYDKSKSQMENLKLPNLKLNFPTTKTVNIVQNIIDETPEEDILKEIQNLREKDKQFFANGNYEVFFAEYNDIPSVMREIGRLRELTFRAVGEGSNLPLDLDNYDKHYHHLFLWDNDKKKIAGAYRMGLGKEIMKKHGIDGFYTASLFEFDQELQPFFRKVIEMGRAFITLEYQQKPLPLFLLWRGIVHVCLRNPDHKFLMGGVSISSKFSDFSKSLMIEFMRSNYYDSAVAQYIHPKNEYKVKLKDRDKSLFLDEMNADLNKLDKIIDDLEPELRLPVLIKKYIKQNAKVVSFNVDPSFNDAIDGLMYIRISELPESTIKPVLEELSEQLRNEQNEIQ
>NZ_CP029149.1|WP_160224301.1|1319979_1321218_+|aspartate-kinase
MKVFKFGGASVKDADSVSNVAKVLESQTFDKCLLVVSAMGKTTNALERVVEDYFQNVDYKIGVEEIKDFHIKIASGLFPEHHKVFAEIALFFDDIDAFLRRNKSPNYNFVYDQVVSCGELISSKILSEYLNQKGFANQWLDARDYIKTDNTSREGQVDWEATEALISTLGLSQSYVTQGFIGSDAHNFSVTLGREGSDYSAAIFAFCLNAETLTIWKDVPGVMTGDPRKFKEATLLSNISYEEAIEMAYYGASVIHPKTLQPLKQKNIPFFVKSFLEPEKAGTKVGSGSDNEYRESYILKENQILVRISTKNFSFIAEEHLSFIFSLLAKYKIKISLMQNSAISLALCLEDKYAHIDEFNRDLGKEFKTEIIPKVSLFTVRNADTNNTLKFYENKTVLLEQISKRTIQMVIQ
>NZ_CP029149.1|WP_160224300.1|1319507_1319669_-|hypothetical-protein
MEKKKTKKEDNKKVRWVIDPETGKKISKTGYAMRLSWKQGGMIKILDMKAVLK
>NZ_CP029149.1|WP_160224299.1|1319088_1319490_-|type-II-toxin-antitoxin-system-VapC-family-toxin
MDTNTLIFAISDREQLSNDILNLLDDYSNILYTSSICIVELLQLYRIEKISTQYKTAGEMIQAIEDDFYIEILPFTKQHTKLLSKLEIADGHNDPFDHAIISQAIAEKLNVISSDRKFEKYTPQKLLFTYNKR
>NZ_CP029149.1|WP_120489493.1|1330502_1332617_+|TonB-dependent-receptor
MRLDGKLFLGSILLISISAIAQNKEKIRERNIKEVVITGQISPQSVKESIKNVRVITAQDIKNMGAVNLDDALNQYINITVLPDVNSGRSTVSLFGLDSSYFKIFIDNIPFVSEGGVGNNTDLSQININDIERVEIIEGSMGVTHGANAVSGILNIITKKKAQSRYEISASVQEESMGNEYNLKDKGRHIQSLKVNYNINDNWMFSTGFNRNQSNGYFGNYKGKNYLLPDGRRGYKFLPRDYTQENALISYRKGSFKSFYKFEYMETNFNFFDRNSKSGYNDEIGAYRYGTDKKYYYSRNAHHLNANGRFNDFAYNISASYQYQEREIERFRYIINTRQSINRERKKDQSMDVIYSTGTLSKSFADKRYNIQLGYELVNNKGFSEVDDAGHTIKQINKKIDNYDVFALSEIGFTKNFSIRPGFRYSFQTLFNNQYSYSLGLRYLLNDYEFRASGGKSYRTPSFDELYTYNVFEGHSFLGNENLIPENGFSTEASIKKTTELNNGKSRLHNQVMFSTNNISDKIYNALLDLDGNAPKFQYINISKYKSYHISTSNNFKSDNWDFGLGASFAWVSQKVESEKHHTDDRFLLNINANLNLSYNIPQWDTRISAYYKFIGKSQQWTVSTKGYVISEQDPYGWLDMSLQKKFFKKNVEVAFGARNLLNTTDIKRTTTSADGSSRNVQSVALGYGRSFYLKLTYNLNIKQ
>NZ_CP029149.1|WP_160224310.1|1332630_1333788_+|hypothetical-protein
MRKNVIITTLAAVTLMLTSCSSTEDGQDGIAEVPSIPPGSLLTLKPEVGGHNQPNQVYVDLRTNTTKVVRRDSWDFGFYCGEDFRVILNGSVKMSTKALNSTNIDEVQSIDNSILISSPGPNTTEVTKASLGYVDNPSGKLKEDNGQKGSGTAIAEISANDSENKVYLVSMGYEISNKNPQPGSIDLTGEHRGWKKIRVLKRANGYLLQYADLADTQHKEFFIEKDSEYNFKFFSIKANNTVDVQPKKKDWDLCFTTNYTYTALVANAPFDKQFVYFFPDLIQLNVHGGVRAAGLQVDRYEKEKIFQAYNLEKANKIDFETPKRINQNFMATAWRKGGLGETAVAEDLIFVVKDSEGNKYKLIFRAVSSESGERGHPVFQYVLLK
>NZ_CP029149.1|WP_160224311.1|1333864_1334503_+|rhodanese
MKSTKFLFPLILLLSFFTSVARAQSLSEVINSKDAVLVDVRSEKEFDEGSVKGAINIPVDTIDKQVYQLKGKKVVVFCRSGKRAEKAYQILKKQGVNVYNGKTVDNVKMLQKSNIIQKVKFLKDKPSVFVIKSGSTAKQVAVALGKDAVLPNHTTSEPALLVVLRGKVKFIIAGEEILLNTYDTYHIPADIEHELVGLDKENLFTVTKSKDW
>NZ_CP029149.1|WP_160224312.1|1334726_1335080_-|TerB-family-tellurite-resistance-protein
MLQKSNKSIAGYHLLMILSAVDHHFSPEEGLKIREYLEEEFPFRINLDNELDIIARLQPEEWKDHFEFHSHCFYDDSTEEERLKFADFAKTLIKADNEVTDREHKFYKLMKHIWKLE
>NZ_CP029149.1|WP_160224313.1|1335084_1336143_-|DoxX-family-protein
MKDALRIIVGVIFIISGFVKTIDARGFSFKLEEYFSPSVFNLSLLETYALPLAIFVAIFEILLGLALVIKLCLKKSLALLIALCVFFAFLTFYSAYFDKVTDCGCFGDAIKFTPWQSFWKDIILLVGLLILWIGYRKEKEQKNKLALAFFFIGLLGTIVITSAGIYGEPLIDFRDYKIGTDLNAERKKIEKNPAEYKTYYTLKNTKTGEEKEANQDDYVNKQEYWEEGTPWEIIEDKTISKLVKEGYKSEISKFKLSDKDENDATEEILNKEKVILIFSYNPKEIKDYSAKISELKKKNSEIYGVSPEGDTFKGLTNFSMDGTAIKTIARSNPFVLVLEKGKIVDKQPLKNY
>NZ_CP029149.1|WP_160224314.1|1336146_1336695_-|DUF1599-domain-containing-protein
MQKTSEQFKKIIAECRDLFSKKMKDYGVAWRVLRPSSITDQIYIKVNRIRTLQMSAKRMIDESEEGEFIAIVNYAIIGLIQMEKGLTDNLNESPEEILNLYDKYASEAQLLMEKKNHDYGEAWREMRVSSITDLIYQKVLRTKQIEDNNGATLVSEGLDANYFDMLNYAVFCLIKSSEESKK
>NZ_CP029149.1|WP_160224315.1|1336756_1338103_-|sulfite-exporter-TauE/SafE-family-protein
MPHSQRKHIRLSLKSEYLRVLIIGEPELIMDELPLLYDKDLEDLQIFAPEETESLRNFAEEMPNTTLHTGIPNDSDFEKAHIAYILTKDETEKINLIHLAKKHKIIIIDELAPSSKHKNTKEKLILNKVQSTIPGTRNYQNPYEVLEYMTTYTKMAKIRATMYLSLIGIMVFAGLFFLTIYEFELYPEVKDFLGRDHSIFYWMLLVGFLAEMVAGSMGMGYGTICTAILLFLGQSPAVASASIHSAQTFTTFAGVASHYKLRNINMKLVKALAPYAILGALMGSFSLYFIDKEYGKIMKPLLAGYTMFIGVNIFIRTLMNQRKRQNINRKRSNLPVLGLVGGFLDSFAGGGWGPLVTGSLIKDGRTPRYVVGSSIFLKFLLTTTSAITFIFTLGTQHWNIILGLLLGGVITAPFSAMLTTRLPIKKMTLAISILVIIMSAITLYKALF
>NZ_CP029149.1|WP_120489486.1|1338220_1339465_-|GTP-binding-protein
MDILRFITAGSVDDGKSTLIGRLLYDSKSILADQLEALEQQSKNKNAEGIDLAILTDGLRAEREQGITIDIAYRYFATPKRKFIIADAPGHIQYTRNMITGASNSELIIILVDARNGVTEQTRRHSIIASLLNIKNVVVAVNKMDLVNYDEDIFTKIKTDYQEIAHRLGLQQVSFFPISAFVGDNIVNTSEAMPWYKGESLLHYLETVEISHREYEQSRFQVQYVIRPQTEELHDYRGYAGQIISGTYAKGDEVIIYPQEQKTRISKIESAGEEVEQAFAHQPVVLHIEDDIDISRGDFFIKADETQPLINNDVEALVCWLDKRELSEGSKCLLQHRSRILKTIVKEIEYKIDVNTLEQVPADGTLKLNEIAKIRLRTASPVIYDDFKENETMGSAILIDETSNATVGALMMMR
>NZ_CP029149.1|WP_160224316.1|1339526_1340435_-|sulfate-adenylyltransferase-subunit-CysD
MEKHQFNHLKQLEAESIYIMREVAAQFERPALLFSGGKDSITLVHLAMKAFAPMKIPFPLVHIDTGHNFPEALKFRDELAKNIGAELIIRNVEDTIKAKGLTEPKGKFASRNWLQIHTLLDTIEEFGFDACIGGARRDEEKARAKERFFSVRDEFGQWDPKLQRPELWNIYNGRIHKGENVRVFPISNWTELDVWSYIKAERISLPSIYFAHEREVIEHENRLIAVSEHIQIDEGDRILRKQVRYRTVGDMTCTAAVESSAKTLDEVVAEISASRISERGETRIDDKVTEAAMEDRKKGGYF
>NZ_CP029149.1|WP_120489484.1|1340499_1341195_-|phosphoadenylyl-sulfate-reductase
MQITKDDIQHLEELPLVEALRYIAAKTTGKVVFSTSLGQEDQIITDAIFKNDIPIEVFTLDTGRLFNEHYELLAMNNAKYKGKIKVFFPDPEDVERFVNEKGINAFYHSVENRKECCFIRKVKPLNRALKGAEVWVTGLRAEQSENRENLPIIEWDEERTLYKFNPLIRWTYQEVLSYIAEHKIQDLPLHRKGYISVGCQPCTRPIMEGENPRAGRWWWEESKKECGLHTH

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Crispr_ID: NZ_CP029149_9

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP029149_9

1504038-1506163

Consensus_repeat	Method
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	PILER-CR
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	CRISPRCasFinder
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	PILER-CR
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	PILER-CR

27 spacers

cas2,cas1,cas9,DEDDh

The CRISPR arrays of NZ_CP029149_9

>merge|NZ_CP029149|9|1504038-1506163|PILER-CR,CRISPRCasFinder,PILER-CR,PILER-CR
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACTGATCGGGTGTCAGGCATGAGGCGGTCGATGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACAGTCCTACAGAATAAGCTTCCAGGTCTACTGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACCACCTGAGCTACCAAGAAGATGCAGGGCTAGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACTGCGTCAAAGATGAGTTTGAGGAGCCCATTGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACCTATTTCCAGTTCTTCTGGTAGGGAGTATAGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACACTCCGTTTTCATCATAGTAATCTGTTACGGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACGCTGGATCTATTATTTTGATGGTAGTGATTGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACAGTTCTAAATGTAACATTTGAATTACTTTTGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACGGGTTCTCTCTGAGCCCTTTCTTATGGTATGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACTGCTCTGAGTTTATCAAATTCAACTCTAACGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACCAATTCATTTCAGATGCTATTAGAGTAGAGGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACTAATTCTGAGATAATAGAGCTGTTACTCCGGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACATTAAAAAAATAATTGAGGATATAAGCCCTGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACGAACTTCGGAGTGTGCCACTCGGGAAAACTGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACACCTATCTAAATGCTTTAATGAGGCAATGGGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACATTGTTTTAATTGATGCGTCAAATATACGCGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACATCGCATTGATATAATCTGTTCCGTCTGCAGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACCAAGTGTAAAATTTGTATTTTCAAGGTTTCGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACGGGAGATTCTGCTGGGTTTTACAGCAAAAGGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACACACAATAATTTTATGAATACAACAACATTGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACTTTTAACGGCTTTGGTCTCGGCATTCACAAGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACACTGCTCAACTCGATAGCTTCATCTATTTTGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACCAGGACTATTAAAGAGCCTCCACCTCCCTCGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACAATACTTAAAAGGCACTAAATCACCGTATAGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACTAAATGAAAAGAGCATAACAATAAAAGAATGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACTATCCGCTTTTCTTTAGCTACTGGTGACTCGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACGGGAGTTATGAGTCGTGAGACTTACTTTAAGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAATATTTGTTTTG

>NZ_CP029149|9|2|1504038-1504392|PILER-CR
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	TGATCGGGTGTCAGGCATGAGGCGGTCGAT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	AGTCCTACAGAATAAGCTTCCAGGTCTACT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	CACCTGAGCTACCAAGAAGATGCAGGGCTA
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	TGCGTCAAAGATGAGTTTGAGGAGCCCATT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACCTATTTCCAGTTCTTCTGGTAGGGAGTATAGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ACTCCGTTTTCATCATAGTAATCTGTTACG
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	GCTGGATCTATTATTTTGATGGTAGTGATT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	AGTTCTAAATGTAACATTTGAATTACTTTT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	GGGTTCTCTCTGAGCCCTTTCTTATGGTAT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	TGCTCTGAGTTTATCAAATTCAACTCTAAC
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	CAATTCATTTCAGATGCTATTAGAGTAGAG
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACTAATTCTGAGATAATAGAGCTGTTACTCCGGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ATTAAAAAAATAATTGAGGATATAAGCCCT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	GAACTTCGGAGTGTGCCACTCGGGAAAACT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ACCTATCTAAATGCTTTAATGAGGCAATGG
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ATTGTTTTAATTGATGCGTCAAATATACGC
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ATCGCATTGATATAATCTGTTCCGTCTGCA
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	CAAGTGTAAAATTTGTATTTTCAAGGTTTC
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	GGGAGATTCTGCTGGGTTTTACAGCAAAAG
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ACACAATAATTTTATGAATACAACAACATT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	TTTTAACGGCTTTGGTCTCGGCATTCACAA
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ACTGCTCAACTCGATAGCTTCATCTATTTT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	CAGGACTATTAAAGAGCCTCCACCTCCCTC
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	AATACTTAAAAGGCACTAAATCACCGTATA
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	TAAATGAAAAGAGCATAACAATAAAAGAAT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	TATCCGCTTTTCTTTAGCTACTGGTGACTC


>NZ_CP029149|9|8|1504038-1506163|CRISPRCasFinder
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	TGATCGGGTGTCAGGCATGAGGCGGTCGAT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	AGTCCTACAGAATAAGCTTCCAGGTCTACT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	CACCTGAGCTACCAAGAAGATGCAGGGCTA
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	TGCGTCAAAGATGAGTTTGAGGAGCCCATT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	CTATTTCCAGTTCTTCTGGTAGGGAGTATA
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ACTCCGTTTTCATCATAGTAATCTGTTACG
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	GCTGGATCTATTATTTTGATGGTAGTGATT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	AGTTCTAAATGTAACATTTGAATTACTTTT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	GGGTTCTCTCTGAGCCCTTTCTTATGGTAT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	TGCTCTGAGTTTATCAAATTCAACTCTAAC
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	CAATTCATTTCAGATGCTATTAGAGTAGAG
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	TAATTCTGAGATAATAGAGCTGTTACTCCG
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ATTAAAAAAATAATTGAGGATATAAGCCCT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	GAACTTCGGAGTGTGCCACTCGGGAAAACT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ACCTATCTAAATGCTTTAATGAGGCAATGG
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ATTGTTTTAATTGATGCGTCAAATATACGC
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ATCGCATTGATATAATCTGTTCCGTCTGCA
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	CAAGTGTAAAATTTGTATTTTCAAGGTTTC
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	GGGAGATTCTGCTGGGTTTTACAGCAAAAG
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ACACAATAATTTTATGAATACAACAACATT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	TTTTAACGGCTTTGGTCTCGGCATTCACAA
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ACTGCTCAACTCGATAGCTTCATCTATTTT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	CAGGACTATTAAAGAGCCTCCACCTCCCTC
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	AATACTTAAAAGGCACTAAATCACCGTATA
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	TAAATGAAAAGAGCATAACAATAAAAGAAT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	TATCCGCTTTTCTTTAGCTACTGGTGACTC
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	GGGAGTTATGAGTCGTGAGACTTACTTTAA
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAATATTTGTTTTG

>NZ_CP029149|9|3|1504423-1504931|PILER-CR
	TGATCGGGTGTCAGGCATGAGGCGGTCGAT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	AGTCCTACAGAATAAGCTTCCAGGTCTACT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	CACCTGAGCTACCAAGAAGATGCAGGGCTA
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	TGCGTCAAAGATGAGTTTGAGGAGCCCATT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACCTATTTCCAGTTCTTCTGGTAGGGAGTATAGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ACTCCGTTTTCATCATAGTAATCTGTTACG
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	GCTGGATCTATTATTTTGATGGTAGTGATT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	AGTTCTAAATGTAACATTTGAATTACTTTT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	GGGTTCTCTCTGAGCCCTTTCTTATGGTAT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	TGCTCTGAGTTTATCAAATTCAACTCTAAC
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	CAATTCATTTCAGATGCTATTAGAGTAGAG
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACTAATTCTGAGATAATAGAGCTGTTACTCCGGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ATTAAAAAAATAATTGAGGATATAAGCCCT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	GAACTTCGGAGTGTGCCACTCGGGAAAACT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ACCTATCTAAATGCTTTAATGAGGCAATGG
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ATTGTTTTAATTGATGCGTCAAATATACGC
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ATCGCATTGATATAATCTGTTCCGTCTGCA
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	CAAGTGTAAAATTTGTATTTTCAAGGTTTC
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	GGGAGATTCTGCTGGGTTTTACAGCAAAAG
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ACACAATAATTTTATGAATACAACAACATT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	TTTTAACGGCTTTGGTCTCGGCATTCACAA
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ACTGCTCAACTCGATAGCTTCATCTATTTT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	CAGGACTATTAAAGAGCCTCCACCTCCCTC
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	AATACTTAAAAGGCACTAAATCACCGTATA
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	TAAATGAAAAGAGCATAACAATAAAAGAAT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	TATCCGCTTTTCTTTAGCTACTGGTGACTC


>NZ_CP029149|9|4|1504962-1506086|PILER-CR
	TGATCGGGTGTCAGGCATGAGGCGGTCGAT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	AGTCCTACAGAATAAGCTTCCAGGTCTACT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	CACCTGAGCTACCAAGAAGATGCAGGGCTA
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	TGCGTCAAAGATGAGTTTGAGGAGCCCATT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACCTATTTCCAGTTCTTCTGGTAGGGAGTATAGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ACTCCGTTTTCATCATAGTAATCTGTTACG
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	GCTGGATCTATTATTTTGATGGTAGTGATT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	AGTTCTAAATGTAACATTTGAATTACTTTT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	GGGTTCTCTCTGAGCCCTTTCTTATGGTAT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	TGCTCTGAGTTTATCAAATTCAACTCTAAC
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	CAATTCATTTCAGATGCTATTAGAGTAGAG
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAACTAATTCTGAGATAATAGAGCTGTTACTCCGGCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ATTAAAAAAATAATTGAGGATATAAGCCCT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	GAACTTCGGAGTGTGCCACTCGGGAAAACT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ACCTATCTAAATGCTTTAATGAGGCAATGG
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ATTGTTTTAATTGATGCGTCAAATATACGC
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ATCGCATTGATATAATCTGTTCCGTCTGCA
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	CAAGTGTAAAATTTGTATTTTCAAGGTTTC
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	GGGAGATTCTGCTGGGTTTTACAGCAAAAG
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ACACAATAATTTTATGAATACAACAACATT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	TTTTAACGGCTTTGGTCTCGGCATTCACAA
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	ACTGCTCAACTCGATAGCTTCATCTATTTT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	CAGGACTATTAAAGAGCCTCCACCTCCCTC
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	AATACTTAAAAGGCACTAAATCACCGTATA
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	TAAATGAAAAGAGCATAACAATAAAAGAAT
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC	TATCCGCTTTTCTTTAGCTACTGGTGACTC
GCTGTGTGATATCCACAAAAGTAATCAAATTGAAAGCAATTCACAAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP029149.1\|WP_120489363.1\|1495604_1497626_-\|recombinase	unknown	unknown	gnl\|CDD\|378408
NZ_CP029149.1\|WP_160224392.1\|1506267_1506816_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_120489353.1\|1512313_1513792_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|225179
NZ_CP029149.1\|WP_160224395.1\|1509707_1511234_+\|T9SS-type-A-sorting-domain-containing-protein	unknown	unknown	gnl\|CDD\|316139
NZ_CP029149.1\|WP_120489352.1\|1513894_1514284_+\|DUF2809-domain-containing-protein	unknown	unknown	gnl\|CDD\|378530
NZ_CP029149.1\|WP_160224393.1\|1506849_1509117_+\|T9SS-type-A-sorting-domain-containing-protein	unknown	unknown	gnl\|CDD\|316139
NZ_CP029149.1\|WP_120489361.1\|1497974_1498310_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_120489358.1\|1503641_1503980_+\|CRISPR-associated-endonuclease-Cas2	cas2	COG3512_cas2_CAS-II-A:CAS-II-B:CAS-II-C	gnl\|CDD\|226043
NZ_CP029149.1\|WP_160224388.1\|1493304_1494540_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|340863
NZ_CP029149.1\|WP_160224394.1\|1509125_1509680_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_160224387.1\|1488592_1493212_+\|DNA-polymerase-III-subunit-alpha	DEDDh	cd06127_DEDDh_CAS-I	gnl\|CDD\|235554
NZ_CP029149.1\|WP_160224391.1\|1502751_1503645_+\|type-II-CRISPR-associated-endonuclease-Cas1	cas1	cd09720_cas1_CAS-II-A:CAS-II-B:CAS-II-C	gnl\|CDD\|274694
NZ_CP029149.1\|WP_160224396.1\|1511375_1512293_-\|cation-transporter	unknown	unknown	gnl\|CDD\|224151
NZ_CP029149.1\|WP_120489727.1\|1488151_1488442_-\|N-acetyltransferase	unknown	unknown	gnl\|CDD\|379642
NZ_CP029149.1\|WP_120489364.1\|1495269_1495566_+\|DUF721-domain-containing-protein	unknown	unknown	gnl\|CDD\|377496
NZ_CP029149.1\|WP_160224397.1\|1514428_1517116_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|366183
NZ_CP029149.1\|WP_160224398.1\|1517534_1519064_-\|2,3-bisphosphoglycerate-independent-phosphoglycerate-mutase	unknown	unknown	gnl\|CDD\|235463
NZ_CP029149.1\|WP_160224389.1\|1494690_1495263_+\|pyruvate-decarboxylase	unknown	unknown	unknown
NZ_CP029149.1\|WP_160224717.1\|1519974_1520700_+\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|276809
NZ_CP029149.1\|WP_160224390.1\|1498472_1502738_+\|type-II-CRISPR-RNA-guided-endonuclease-Cas9	cas9	cd09643_cas9_CAS-II-A:CAS-II-B:CAS-II-C	gnl\|CDD\|375967

Protein	Function_ID	Function_description	E-value
NZ_CP029149.1\|WP_120489363.1\|1495604_1497626_-\|recombinase	gnl\|CDD\|378408	pfam10136, SpecificRecomb, Site-specific recombinase. Members of this family of bacterial proteins are found in various putative site-specific recombinase transmembrane proteins.	1.76796e-176
NZ_CP029149.1\|WP_160224717.1\|1519974_1520700_+\|tetratricopeptide-repeat-protein	gnl\|CDD\|276809	sd00006, TPR, Tetratricopeptide repeat. The Tetratricopeptide repeat (TPR) typically contains 34 amino acids and is found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans. It is present in a variety of proteins including those involved in chaperone, cell-cycle, transcription, and protein transport complexes. The number of TPR motifs varies among proteins. Those containing 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accommodate an alpha-helix of a target protein. It has been proposed that TPR proteins preferentially interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes.	1.07318e-14
NZ_CP029149.1\|WP_120489353.1\|1512313_1513792_-\|MFS-transporter	gnl\|CDD\|225179	COG2270, COG2270, Permeases of the major facilitator superfamily [General function prediction only].	2.66329e-74
NZ_CP029149.1\|WP_160224395.1\|1509707_1511234_+\|T9SS-type-A-sorting-domain-containing-protein	gnl\|CDD\|316139	pfam13583, Reprolysin_4, Metallo-peptidase family M12B Reprolysin-like. This zinc-binding metallo-peptidase has the characteristic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.	1.07739e-16
NZ_CP029149.1\|WP_160224393.1\|1506849_1509117_+\|T9SS-type-A-sorting-domain-containing-protein	gnl\|CDD\|316139	pfam13583, Reprolysin_4, Metallo-peptidase family M12B Reprolysin-like. This zinc-binding metallo-peptidase has the characteristic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.	1.01026e-15
NZ_CP029149.1\|WP_160224396.1\|1511375_1512293_-\|cation-transporter	gnl\|CDD\|224151	COG1230, CzcD, Co/Zn/Cd efflux system component [Inorganic ion transport and metabolism].	1.46628e-79
NZ_CP029149.1\|WP_120489358.1\|1503641_1503980_+\|CRISPR-associated-endonuclease-Cas2	gnl\|CDD\|226043	COG3512, COG3512, CRISPR-associated protein, Cas2 homolog [Defense mechanisms].	2.11058e-23
NZ_CP029149.1\|WP_160224388.1\|1493304_1494540_+\|MFS-transporter	gnl\|CDD\|340863	cd06173, MFS_MefA_like, Macrolide efflux protein A and similar proteins of the Major Facilitator Superfamily of transporters. This family is composed of Streptococcus pyogenes macrolide efflux protein A (MefA) and similar transporters, many of which remain uncharacterized. Some members may be multidrug resistance (MDR) transporters, which are drug/H+ antiporters (DHAs) that mediate the efflux of a variety of drugs and toxic compounds, conferring resistance to these compounds. MefA confers resistance to 14-membered macrolides including erythromycin and to 15-membered macrolides. It functions as an efflux pump to regulate intracellular macrolide levels. The MefA-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	5.31458e-57
NZ_CP029149.1\|WP_160224398.1\|1517534_1519064_-\|2,3-bisphosphoglycerate-independent-phosphoglycerate-mutase	gnl\|CDD\|235463	PRK05434, PRK05434, 2,3-bisphosphoglycerate-independent phosphoglycerate mutase.	0
NZ_CP029149.1\|WP_160224387.1\|1488592_1493212_+\|DNA-polymerase-III-subunit-alpha	gnl\|CDD\|235554	PRK05673, dnaE, DNA polymerase III subunit alpha; Validated.	0
NZ_CP029149.1\|WP_160224391.1\|1502751_1503645_+\|type-II-CRISPR-associated-endonuclease-Cas1	gnl\|CDD\|274694	TIGR03639, cas1_NMENI, CRISPR-associated endonuclease Cas1, subtype II/NMENI. The CRISPR-associated protein Cas1 is virtually universal to CRISPR systems. CRISPR, an acronym for Clustered Regularly Interspaced Short Palindromic Repeats, is a prokaryotic immunity system for foreign DNA, mostly from phage. CRISPR systems belong to different subtypes, distinguished by both nature of the repeats, the makeup of the cohort of associated Cas proteins, and by molecular phylogeny within the more universal Cas proteins such as this one. This model is of type EXCEPTION and provides more specific information than the EQUIVALOG model TIGR00287. It describes the Cas1 variant of the NMENI subtype of CRISPR/Cas system.	9.5755e-91
NZ_CP029149.1\|WP_120489352.1\|1513894_1514284_+\|DUF2809-domain-containing-protein	gnl\|CDD\|378530	pfam10990, DUF2809, Protein of unknown function (DUF2809). Some members in this family of proteins are annotated as yjgA however currently no function for the protein is known.	3.09582e-20
NZ_CP029149.1\|WP_120489727.1\|1488151_1488442_-\|N-acetyltransferase	gnl\|CDD\|379642	pfam14542, Acetyltransf_CG, GCN5-related N-acetyl-transferase. This family of GCN5-related N-acetyl-transferases bind both CoA and acetyl-CoA. They are characterized by highly conserved glycine, a cysteine residue in the acetyl-CoA binding site near the acetyl group, their small size compared with other GNATs and a lack of of an obvious substrate-binding site. It is proposed that they transfer an acetyl group from acetyl-CoA to one or more unidentified aliphatic amines via an acetyl (cysteine) enzyme intermediate. The substrate might be another macromolecule.	7.37359e-28
NZ_CP029149.1\|WP_120489364.1\|1495269_1495566_+\|DUF721-domain-containing-protein	gnl\|CDD\|377496	pfam05258, DUF721, Protein of unknown function (DUF721). This family contains several actinomycete proteins of unknown function.	0.00180172
NZ_CP029149.1\|WP_160224397.1\|1514428_1517116_+\|TonB-dependent-receptor	gnl\|CDD\|366183	pfam00593, TonB_dep_Rec, TonB dependent receptor. This model now only covers the conserved part of the barrel structure.	6.78819e-12
NZ_CP029149.1\|WP_160224390.1\|1498472_1502738_+\|type-II-CRISPR-RNA-guided-endonuclease-Cas9	gnl\|CDD\|375967	pfam18541, RuvC_III, RuvC endonuclease subdomain 3. Cas9 proteins are abundant across the bacterial kingdom, but vary widely in both sequence and size. All known Cas9 enzymes contain an HNH domain that cleaves the DNA strand complementary to the guide RNA sequence (target strand), and a RuvC nuclease domain required for cleaving the noncomplementary strand (non-target strand), yielding double-strand DNA breaks (DSBs). The crystal structures of type II-A and II-C Cas9 proteins highlight the features in Cas9 enzymes that support their function as RNA-guided endonucleases. Cas9 enzymes adopt a bilobed architecture composed of a nuclease lobe containing juxtaposed RuvC and HNH nuclease domains and a variable alpha-helical lobe likely to be involved in nucleic acid binding. The RuvC domain forms the structural core of the nuclease lobe, a six-stranded beta sheet surrounded by four alpha helices, with all three conserved subdomains (I, II, III) contributing catalytic residues to the active site.	1.2974e-54

>NZ_CP029149.1|WP_120489358.1|1503641_1503980_+|CRISPR-associated-endonuclease-Cas2
MKNERLNAYRVMWVMVLYDLPTDSKASMKAANLFRKQLVDDGFSLFQFSMYIRHCPSRENAEVHIRRVKDILPKYGKVAIMCITDKQFEGIEIFYSRKQELPPPTWQQLELF
>NZ_CP029149.1|WP_160224391.1|1502751_1503645_+|type-II-CRISPR-associated-endonuclease-Cas1
MLYRSIYIGNPAYLKLKDNQLKIICPESKIEKGSVAVEDLGLLMLDHWQITLSHQLIQKMMEAKVVVISCDTKHLPQGIMLPTNGHTQYSERVKHQIEASEPLKKQLWKQTIECKIQNQIKVLNKLGRFSEPMYDYLKNVKSGDVTNMEGIAAQHYWKNLINPDFLRGRFGDYPNLFFNFGYGVLHSIVARAIVDTGLLLVLGIFHKNKYNPYCLASDIMEPYRPFVDLLVMDWIMQNPKSEELDKEAKNHFLNIASKDILIDRLNRPLIVAVKMTVSSLYKCYTGEKRQISYPEML
>NZ_CP029149.1|WP_160224390.1|1498472_1502738_+|type-II-CRISPR-RNA-guided-endonuclease-Cas9
MKRILGLDLGTTSIGFAYVVEGETPEKSLIKEIGVRVNPLTTDELSNFEKGKSISVNADRTSKRSARRNLQRFKLRREVLIKILKENKIITENTVLAEEGKGTTFQTLKLRAQAAKQKVSLSELARLFLIINKKRGYKSSRKAKNEEEGQLIDGMSIARKLYEQNLTPGQFVYELINKGNKSIPDFYRSDLQNEFDRVWDFQKQFYADILTDEFYIELKGKGQKATSAAFLSKYKIYTAENKGSREEKKLQAYLWRAKAISEKLSKEELAYVITEINNNLNNSSGYLGAISDRSKELYFNKQTVGEYLWEQIQKNPHTSLKNQVFYRQDYLDEFEKIWSTQAQFYPDILTNNLKKEIRDTVIFYQRKLKSQKGLISFCEFESKEIEIVKEDGKLVKKLIGSRVAPRSSPLFQEFKIWQNLHNVTVRKKDSRKRKALETAQELFVDEDKEIFILSLEQKQLLFDELNLKGNLSSSKILELLGLSSKEWELNYKQIEGNKTNRQLYDAYLKIIDLSGHSISDYVKVKSTKSDIQLDDLNIPSLEIKNIVKQIFETINISTDILEFNAELKQKEFEKQASYQLWHLLYSYEGDNSKSGNEKLYKLLEDKFGFKEEYAKILADIIFLTDYGNLSTKAIRKIYPYIKENGFSEACKLAGFKHSKDSLTKEENQQRVLKQRLEPVKKNSLRQPVVEKILNQMVNVVNSLIDKYRKEDENFAFDEIRIELARELKKNAKERAELDTQVRDGKARNEKIIAILKSSEFGIPNPTKNDITRYRLYEELKDNGYKDLYTNRYISRSDLFTNKIDIEHIIPKSRLFDDSFSNKTITFRDVNLKKGDRTAYDFIESNYNSELENYLSRVEDLYQKNIISKAKYQKLLKKESEIGDGFIERDLRETQYIAKKAKEMLLQITKSIVSTSGSITDRLREDWDLVNVMKELNLPKYRALGLTEMQERKFGQKVEVITDWTKRNDHRHHAMDALTVAFTKHTHIQYLNYLNARKDENHKEHNVIINIQNLETEKIKDKNGNEKRVFKEPIPNFRQVVKAYLESVLISHKAKNKVTTKNKNKISGKNNRSQDTLTPRGQLHKETVYGKYHYYVSKEEKVGVKFDNETIEKVANPLFKQLLKARLEENNNDPKKAFTGKNSLEKNPIYLDDSKQKVMPEKVKLVWLEVDYSIRKDINPDNFKTEKLIDKILDEGIKKILKERLKEYDNDPKKAFSDLDKNPIWLNKEKGIAIKRVTISGVKNAEAIHTKKDHLGNEILDKKGNPIPADFIQTGNNHHIAIYRDNKGDLQENVVSFFEAVARAKQGLPIIDKTYNQHLGWTFLFTMKQNEMFVFPNKETGFNPNEIDLLDPKNKKIISPNLFRVQKLSTKDYFFRHHLETNVQMDISLKNITWKRESLIGINNIIKVRINHLGDIVSVGEY
>NZ_CP029149.1|WP_120489361.1|1497974_1498310_-|hypothetical-protein
MRKSVLYFVIGTTISFIINYFILNAGVGWQLNLFYGMAFGLGWGLAYFVDQPKWKLHKKMSISFIGIIILLIIGRLFFNSILVIPSIIRFSTVFVAYYLIASFKQSKSLRQ
>NZ_CP029149.1|WP_120489363.1|1495604_1497626_-|recombinase
MSVLKINRERYNHILERYFTFKNETTSVEPLIQIMKSFRKEKFSIILNFLIHHPEIANNFGYYIQNLFNGKTFNLSLTESNILTENSFFPELKKRVLNAVLPPISNENSIGYIVDNVSVIPSVDLKYFKQIPQEELDKFFELLGISDYITKPSVRRSLLYSANVLAWRVIGNAMDMEVLRMVPEYQNLGNPFLALQNELDTLISEFKQNQNFQLHSKDELTKQLKIYWKQCEEFVDTAFKNSSAYGISGRTNQSLLKIRQQLNRMKEVLMLLVIDEEKDILHNSQKLFLNILEYKSHKNNVKELADDSTRLLSHLITNHTAETGSHYIASGKKAYVNMFWKASGGGVIVGALCVLKMMYSYSPGSEFMHAILYSFNYAMGFIMIYLMHYTLATKQPAMTAATMAKALSLGENSEKNYLAFASVVSKLFRTQFIAFIGNVLWSFPVALVLIYGLDVLFNQNFAVDKADKFLKELNPFESKAILHASLAGFFLFISGIIAGNASNNSVFYQMPERIAKNPMINRIFGNKFANGLSNFYAKNWAGITSNFWFGVCLGVTGPIGKFLGIDIDIRHITFSSGNLALGLYGKGFDVVASTFWIAFITVFIIGFFNFIVSFGLSIVLALRSRKVYFSEFIRISKVTFRYFMENPLRFFIPLKSNLDSSAKEMLDQTVSKK
>NZ_CP029149.1|WP_120489364.1|1495269_1495566_+|DUF721-domain-containing-protein
MKQRKKREYQSSELVKAFAKIYGFENKLLALEVKSFLAEYMGTESFKEIEKVDLKQKKLIIIVKSPILRNDLQFKRSFLLKKIKENFGEDTFETVEII
>NZ_CP029149.1|WP_160224389.1|1494690_1495263_+|pyruvate-decarboxylase
MKRKRLAVFALIFLVGGLGWAGAQVLASGRGMQNFQQEREETVLYFSPEVFPDVEEIKEPTNLAFFSALTDKVASLKGRKVLRVDAMMSFEEISPEIIREYCKNNGASYAVLPRVKYFKVGFGKYVFSNQVVVSMKLYDAEGSLITETEYNTYRKNMRLLGSAENSVQVGTKGAINDLAKKLRKALRKAK
>NZ_CP029149.1|WP_160224388.1|1493304_1494540_+|MFS-transporter
MISLTPLKTLQNAQFRGLLAGRFFLILAFRMLGTLLGWWVYQLTKDPFAIGLIGLSEVIPAVSSALYAGYVIDMNEKKRLLLICNYAYVLLVAVLGLLAFSAEGWGLSNHQITYVIYGVIFFTGISRAFLGPIIPSMIPKIVTKDTLPNAITLNQSTFLTASVGGHAIGGILIGKIGVEWTLIVIMSLMLIASLFFWGLQKQPSENNNQNIRIMESIKEGVLYIYKTKEILGALFLDMFAVLFGGAVAMIPVFATDILKVGAEGFGLLNAATDIGSMLIIITLSFIPLRRNQGKILLMAVAGFGICIIGFGFSKIYWLSFILLMMSGMLDGISVVIRGTIVQLKTPDEIRGRVLSVNSIFIMSSNEMGQFESGLAAKLMGVTRSVIFGGSMTLLIALLVALKNLKLRNMEY
>NZ_CP029149.1|WP_160224387.1|1488592_1493212_+|DNA-polymerase-III-subunit-alpha
MYLVFDTETTGLPQNFDAPISDSSNWPRMVQLAWQIHDENGKLIDNQDFIIKPEGYDIPFNVSQIHGITTSIANEIGDDLETVLKHFAEAVEKCKFGVGQNIDFDYKIVGAEFYRKGIADKLQALPKADTMWLGTQFTAIPQGNTGRLKPPKLEELYEKLYGFKFDEAHNAAADVNATAQVFFEMLRRGIISAADLGVEESVISHFQSLHTEPIKPFPIVIRSQIAEFNKRKQGASQTAQEMDLGSYFNFHNHSIFSSLQASTHHSDMVNKALKNDFPAVGMVDFGNLMGAFKFVNEVEKANGDLKKKHQEFIDNHPDETPPPLKQLIPIIGCEFYISDRPEQKQFTKDDPDRRTNIVLLAKNFRGYKNIAKLSSLGFVNGFYFGVPRVSKEWILQHKEDVIALSSGLNGDIPNAVLEYGETKGEQVFKWWKDAFGEDFYVQIQNHGLAEEEYLNDILLRWAEKYDVKVLAQNETYYTSKEDAHIQEILFCIKDGEKLSTPVGRGFGKRKGLPSKDYDMKDREEIKRAFSHYPTAFKAYEDFLKKFEPYALKREVLLPKFEIPEQFQSEEDEKDGGKRGENAFLRHLTYEGAKRRYEEITDEIRERLDFELEIIANTGYPGYFLIVQDFCNEARNMGVWVGPGRGSAAGSAVAYCIGITNVDPIKYDLLFERFLNPERISMPDIDIDFDDEGRDKIIKWVVEKYGKMNVAQIITYSVLGGKSAITDAGRVLEYSIPDTKGIAKLVPPAPGMNIAKAFKKYEKLPPEDKILVDEMKTILDNKKDARFPVLSAAQKMEGCIRNTGIHACGVIITPEDISNLVPITTAAKDSDVLVSQFDNSVAEAAGLLKMDFLGLRTLSIIRDAIKLIKDNYDIDINPDEISLEDEKTYQLFQEGRTIGIFQYESVGMQKYMRELKPTVFADLIAMNALYRPGPIKYIPNFINRKHGIEEIVYDLPETEEYLKETYGITVYQEQVMLLSQKLANFTKGEADTLRKAMGKKQIDVLNKMYPKFIEGGKKNNLNEEKLEKIWNDWKAFAEYAFNKSHSTCYAYIAYQTAYLKANYPAEYMASVMTHNLNNTKQITMFMEDCKAMGVDVLGPDVNESQYEFSVNDKGQIRFGLGAIKGIGEGPSEIIVETRQQGKFKDIYDFFERIPASQINKRVVESLVVAGAFDEVDEYHRAQYFQEDNANRTTIERLLKYGQSFQESRNEMENSLFADFAEEVQIEQPKIAPAPEWQNMHKLNREKEIIGFYLSSHPLDEFKYQYQFIQGLLSKKEVVETKNTDEEFLDKAQPAYNESQEEADDTLTDELIDIEMGDAEEPVENAAKVIEARGKFRFLNLDELDAYRDKNFGAEQLKLFETVDYKTKQAMNTAVRENMVAGLVTEYLIRDGRNSGEKVAFVTLEDYSGSYSFRLGDRDYLRLKDKIDLQRFLIFKVKYSMSKDGRVYLNVVDVMELKDAFERFANSLSVVVDIQDFRQEDLEFLSKVIQENFGDKKLRFYLRNKENNSHLELNTIRPSIKIDGDFIKFFVENNKFQFYLN
>NZ_CP029149.1|WP_120489727.1|1488151_1488442_-|N-acetyltransferase
MDTIKFEREDDGTTGRFIIYDGEIFAGEMTYKWADSKTLLIDHTRIEEAFGGRGLGKLLVAEAVKFAREQGIKIIPLCPFVKAVFSKVPSLEDVKK
>NZ_CP029149.1|WP_160224392.1|1506267_1506816_+|hypothetical-protein
MKFLNSFLGLVLLAFMQILQAQQSVKSILPLFSQKKQVEWAVQTDRNESVPVKWYERESSFAVEGIRTFVGYYNEQLVGALSVQRNDISGSIQWVGKAYHIDTRQGKVVISTSGADMNCGTCSGNFCASDSAEEKSFLRVDYKKQKFVYTDPVLRVYRLAITIDYSYFSRTFGFNKARVRGY
>NZ_CP029149.1|WP_160224393.1|1506849_1509117_+|T9SS-type-A-sorting-domain-containing-protein
MRDLAMKFKVINDDRLIIDTKDKELFNTTNLYYIISNSTQKINGLIGENNYEVGVMVTEPAKGVLGIATLGGFYNKSTKGSALVSNNNYTLAHEVGHLFGSNHTFSNGPITYSTEPLSGTSIMGYGFKDDDVFFSLVSASKIKERVFYNPGYYSDEEHKHWVGEKSAAIPFYGINTNNRPPLINRAKLQPEYKIPPDTFFQFMIDATDPEDDALLYMAHQADIDQPGKANFIAYSPSKDNTVKYEAKYERVLTNPGNDDGEDEYEIQKVPYSSPEPSDRGVYTFWLGVSDGGRKAHQQPHATQYDIEKVNLNIVDGTPFKITSVMPLSNMEEGDTITIKWDVDRNIFGNDTKVRILFSDDYGKTYKYVLADEVPNNGEYKVSLPAGIRKAGKVWSWGSERTKHKVEGIFKVEVIDHIAYALYTRRSLKEPSPMEVYEPKIVFKNLPEPVITVKKTEIPPKAEVTATSSCSGTGNNIPNIDYEEENHLHYILRKWEATDNCGNKNSFTQYIYIEKDRLKFVGDLPKDIHFQCKDSQLPEVPKLEVTGGDESTKIEFTEEKIDLWNGNYKLIRSWYASADKVSPVAHSQVILVQDTTPPELSDYPKDQIVKTEADIPAQQGLTAVDNCDGAVKVSQGWEAGELNGKKQKKYVWLAEDRSGNVNRYVQTFTIDPDDAGLSTDEVEVKSLRIYPNPFKDSFVVEGVEGDFNLKIYDLSGKQFKSFGKMQRYIVSDLPAGVYIVNVEADNILHTFKIIKK
>NZ_CP029149.1|WP_160224394.1|1509125_1509680_+|hypothetical-protein
MNIKKTFFVLLLLGLVQNLCAQKVRDIVRLFHRSEAISWAVPLPGNPLTIQWQERETAFSREGIRTFVGYSNGNLIGTLSIRPNAVSGNLSYNGKEYFINTDNGELHYTEENHSEEGQCGTDELIHQSESAKRYLDTVSEGSEAPQIKNTEILRVYRLAIAVAYNRYSDYYFNSDVQKVKDFWA
>NZ_CP029149.1|WP_160224395.1|1509707_1511234_+|T9SS-type-A-sorting-domain-containing-protein
MRDLGIRFELINDEKLIIKDAANEMVYDYHTPEYIISYATRNIGALIGDKNFDSGLWLSGFSRTGIVGLAYIFGAYDSGKAAAVVSNYSKETIAHEIGHLFGGRHTFSTQVVQSDSEKTELGRGQSVMSYGAPRNFFSLSSIQRMRERITTLPYYIDKKRTQVRGDANFPNIPYGEQLTNTPPVIDKSKLKTEYIIPKNTFFQFYIPATDADGDALSYSAQQRDVRLLNSPSISIYKAYKPTQTNPVSFQREYDTNLRGGAIYDSQPPQDTTGEFSFWLAASDPKMSTQNHFITNFDLAQTTVKVIEGKPFKITTAIKKKYKGGEKINLNWEVDEAIFGADSKVRILLSDDWGQTFKYTLAEEVENNGNYEVTLPNINIGEIEVGSAKLKVNAGIIKVEVIDRLAFDITEKAPSARGGFIVEEDPSLATEITDLKSSDILIYPNPVKSSFSLKGLPQSSKIKVFDINARLLKSFAPQQNYDVSELSNGNYILSIETPKGALHLKFIKQ
>NZ_CP029149.1|WP_160224396.1|1511375_1512293_-|cation-transporter
MEHSHEGHCHHSVSSLDAINRAFYIGIGLNLLYTIVEYGVGFSINSLALISDASHNLSDVASLIISLLGMKLAQKAASRTYTYGYKKASILASLINAILLVFIVANICIEAVERLSLPPNVKGLDISITAFVGVMINSISAFLFYKGQKQDINIKGAFLHLMVDALVSVGVIISGVIISLTGWNAADIFISFVIAAVILISTWHLLTESLKLILDGVPADINTKEIQQAIEQHPMIDSLHHLHIWAMSSSQNALTAHIVLAQEISLADTEQIKKELRHTLAHKNIHHSTFEMEVKGCHCKQEECD
>NZ_CP029149.1|WP_120489353.1|1512313_1513792_-|MFS-transporter
MSQNRTKTTSKTGIKNNPKIMNAWAAYDWANSVYSLVITSTIFPIYYSLLTTKGYKKEFIESTQQWIKVPERYFLKIFGEAYHPDAVYGYSLTASFIIVVLLSPFLSSLADTIGNKKSFLQFFCYLGATSCMGLAIFTGMNTVFLGLLFSITASVGFWGSLVFYNSFLPDIASPDRQDALSARGYVYGYVGSVVLVIICLLLIKVAAQTAEESKLYTRVSFLLTGAWWFGFSQYTFKHLPQFGSVKDNLPKDLVLLNYTNIFKKHAKQGGFFTVLMDNIRFYIDIGKQSFKELFKVQKQLFEDRNLKFFLSSFFFYSVGMQTIFLMATLFGSNEINLEQGKLIATLLIIQIEAIIGAIVFSKLSQRIGNKNVISITVILWIVACLGSYLLNKENPNVEYQFYGIAGIIGLVMGGLQALSRSTYSKLLPENSMDNTTFFGFYDVLEKLAIIFGTFIFSALIDHFNNMRYAALSMSFFFFIGLVLIRFIKAKKS
>NZ_CP029149.1|WP_120489352.1|1513894_1514284_+|DUF2809-domain-containing-protein
MRFNLRYGLLSLIIFGIEVCIATIWKDIFLLRAYIGDVLVVMLLYTAILSFFNIKNKGTLLIYIFLFSVLVEVAQYFKLATLLGFKEGSIMYIVIGNSFSWLDILCYFIGVLLMYLGLGSKLYAVGSKQ
>NZ_CP029149.1|WP_160224397.1|1514428_1517116_+|TonB-dependent-receptor
MKRRKILFFGFLLLMGLSYAQVVQGVVLDKETGKSLQNVKISPEGTDSWTLTDANGSFKIDLKGHKELVFILSGYTEIKQRAEENMEVLLSPATIYIKEVQLTAKRRRFSEIDIKEEAIKNNQSFSIADVLTQLPGQFIKPLNNNEFKNVVFRTGSGQSLNNRNNDSYGNKAAGVSVLVDGLAVSNNENMQQYNSPYSAVYRGLSSRTDIPTPSLPNYGADLREITVGDIENIKVVQGIPDAKYGDLTTGLIIVETKSGKKPLQINASLQRGTYQVDVTKGFQINKKGDAINFLINYMDANPNPRNNLTDYKRIVGKILWEMSSRDKTVRNKINFQYAKNLDEGKTDPDDYKARYVKASKVGFVLSDNFTMKFKDRWIDGLSANVRFSYDKQKNIDKQFVNLGGRPYGTAMENSVYYAPYTPVTFMTERNVEGIPINLNMNVEMYKLIESRNKWRHNISAGGAFIFGDNIGRGRFGTTNSAIVGISNAASNMGYRDYDYSKNVPASVQYSAYLQDNLRKDIGEYSSLSLNAGLRLDIQNSIKTLSPRFNASYKYKNISLRGGVGLTSKAPTLAQLYTGDRFLDYLIGDFRLPGKYNVAVMQTVVTKGDNVDLKPSKSWKTEVGLDYKFPFAMLSFTAYYNKLFDGFTNVSELNKTQISDVKINYNGNQPPTYQIIGQKDYYYTHSRITNALNSVDKGIELGINFKRIEALNLEVALNATYVRTDDKSDVRYLQKSNIETSEYTYGVFTAGGNAFENARINGTFAYHLSQVGLILALQTNTFLLDNFYVDANNKYPEGYYDRNLTYHPIPESERADAKYQNIHRQATETTTQRLGKVLHNIHLRVTKNFLSGFQASVYVYNVLNSRPARKNLNNGSIEEYDFFTPISFGANLSYKF
>NZ_CP029149.1|WP_160224398.1|1517534_1519064_-|2,3-bisphosphoglycerate-independent-phosphoglycerate-mutase
MAHKALLAILDGWGLGKDPKISAIDQAKTPFMDSFYQKFPHTTLEASGMAVGLPAGQMGNSEVGHMNLGAGRVVYQNLVKLNMAVENKTLGKEPAILSAFQYAQENNAAVHFIGLCSDGGVHSHINHLKGLLSAAKDFGLRDNVFVHAFTDGRDCDPHSGKGFITDLQSFMNQNVGKLATIVGRYYAMDRDKRWERVKLAYDVMVNATGTPAQDAVEAIQKSYDEGISDEFLKPIVCIDEHQNPIAKIKDGDVVFCFNFRTDRGREITEVLSQQDFPDFGMHKLSLHYITMTNYDSEFKGVQVVFDEEVLTHTLGEILEANGKRQIRTAETEKYPHVTFFFSGGREEPFNGEKRILCPSPKDVATYDLKPEMSAYDITKNILPEIEQESADFICLNFANTDMVGHTGVFSAAVKAAETVDECIGKVATTAYEHGYTVFILADHGNSDVMLNPDGTPNTQHSTNLVPLIVMDKDKTWTLRPGKLGDVAPSILTAMGITIPKEMTGEVIIE
>NZ_CP029149.1|WP_160224717.1|1519974_1520700_+|tetratricopeptide-repeat-protein
MRKIYSLLVFFVFFATAQERYKTSIFEGNRAFEKENYDEASAKFMQAVKQKEKDFSAHYNLGNALYKGKKYDEAMAEYKKAEANAKTKQDKMAAHYNLGNAYMQSGNPAKAAEYYKKALKNDPYNEKVRKNYEIAKLKDKENQQSQQNQNQQDKNQQQKDQNNTPKDENNGKPPKGKDQNQQGNDGNTDQKQNKGKNDGERMPKDLEDALLERVKSREQETARKILNKNTYSVPQSNEKDW

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Crispr_ID: NZ_CP029149_10

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP029149_10

1711681-1711791

Orphan

Consensus_repeat	Method
GCACTTAGCCACAGCGTGGCAGGCAATT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP029149_10

>merge|NZ_CP029149|10|1711681-1711791|CRISPRCasFinder
GCACTTAGCCACAGCGTGGCAGGCAATTAGACCGTAGCCGGTGAGGCATCCACTCGCGTGGAGAGCACTCGTTAGCACGAGAGGCACTTAGCCACAGCGTGGCAGGCAATT

>NZ_CP029149|10|9|1711681-1711791|CRISPRCasFinder
GCACTTAGCCACAGCGTGGCAGGCAATT	AGACCGTAGCCGGTGAGGCATCCACTCGCGTGGAGAGCACTCGTTAGCACGAGAG
GCACTTAGCCACAGCGTGGCAGGCAATT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP029149.1\|WP_120489181.1\|1707603_1708680_-\|4-hydroxythreonine-4-phosphate-dehydrogenase-PdxA	unknown	unknown	gnl\|CDD\|273137
NZ_CP029149.1\|WP_160224500.1\|1704527_1705676_-\|T9SS-type-A-sorting-domain-containing-protein	unknown	unknown	gnl\|CDD\|275380
NZ_CP029149.1\|WP_160224501.1\|1705679_1706975_-\|T9SS-type-A-sorting-domain-containing-protein	unknown	unknown	gnl\|CDD\|275380
NZ_CP029149.1\|WP_160224498.1\|1701963_1703274_-\|ribosome-biogenesis-GTPase-Der	unknown	unknown	gnl\|CDD\|234628
NZ_CP029149.1\|WP_160224499.1\|1703381_1704329_-\|methionyl-tRNA-formyltransferase	unknown	unknown	gnl\|CDD\|234567
NZ_CP029149.1\|WP_160224502.1\|1707107_1707470_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_120489175.1\|1713150_1714230_-\|PASTA-domain-containing-protein	unknown	unknown	gnl\|CDD\|275384
NZ_CP029149.1\|WP_160224503.1\|1709525_1710980_+\|HAMP-domain-containing-histidine-kinase	unknown	unknown	gnl\|CDD\|223715
NZ_CP029149.1\|WP_160224728.1\|1711974_1713042_-\|RluA-family-pseudouridine-synthase	unknown	unknown	gnl\|CDD\|223638
NZ_CP029149.1\|WP_160224505.1\|1717650_1719081_-\|cation:dicarboxylase-symporter-family-transporter	unknown	unknown	gnl\|CDD\|234968
NZ_CP029149.1\|WP_160224497.1\|1699690_1701193_+\|GH3-auxin-responsive-promoter-family-protein	unknown	unknown	gnl\|CDD\|377019
NZ_CP029149.1\|WP_120489180.1\|1708931_1709516_+\|riboflavin-synthase	unknown	unknown	gnl\|CDD\|236455
NZ_CP029149.1\|WP_120489174.1\|1714347_1715328_+\|D-alanine--D-alanine-ligase	unknown	unknown	gnl\|CDD\|234993
NZ_CP029149.1\|WP_120489173.1\|1715337_1715796_+\|pantetheine-phosphate-adenylyltransferase	unknown	unknown	gnl\|CDD\|234674
NZ_CP029149.1\|WP_120489168.1\|1719633_1720668_-\|DNA-polymerase-III-subunit-delta	unknown	unknown	gnl\|CDD\|273455
NZ_CP029149.1\|WP_160224506.1\|1719162_1719621_-\|BON-domain-containing-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_160224729.1\|1716912_1717611_-\|SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|381176
NZ_CP029149.1\|WP_160224504.1\|1716030_1716867_-\|RNA-binding-protein	unknown	unknown	gnl\|CDD\|225543
NZ_CP029149.1\|WP_120489167.1\|1720674_1721118_+\|type-I-restriction-enzyme-HsdR-N-terminal-domain-containing-protein	unknown	unknown	gnl\|CDD\|372640
NZ_CP029149.1\|WP_120489187.1\|1701235_1701886_-\|uracil-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|234653

Protein	Function_ID	Function_description	E-value
NZ_CP029149.1\|WP_120489181.1\|1707603_1708680_-\|4-hydroxythreonine-4-phosphate-dehydrogenase-PdxA	gnl\|CDD\|273137	TIGR00557, pdxA, 4-hydroxythreonine-4-phosphate dehydrogenase. This model represents PdxA, an NAD+-dependent 4-hydroxythreonine 4-phosphate dehydrogenase (EC 1.1.1.262) active in pyridoxal phosphate biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine].	3.00366e-133
NZ_CP029149.1\|WP_160224500.1\|1704527_1705676_-\|T9SS-type-A-sorting-domain-containing-protein	gnl\|CDD\|275380	sd00033, LRR_RI, leucine-rich repeats, ribonuclease inhibitor (RI)-like subfamily. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions.	1.0968e-13
NZ_CP029149.1\|WP_160224501.1\|1705679_1706975_-\|T9SS-type-A-sorting-domain-containing-protein	gnl\|CDD\|275380	sd00033, LRR_RI, leucine-rich repeats, ribonuclease inhibitor (RI)-like subfamily. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions.	4.3703e-17
NZ_CP029149.1\|WP_160224498.1\|1701963_1703274_-\|ribosome-biogenesis-GTPase-Der	gnl\|CDD\|234628	PRK00093, PRK00093, GTP-binding protein Der; Reviewed.	0
NZ_CP029149.1\|WP_160224499.1\|1703381_1704329_-\|methionyl-tRNA-formyltransferase	gnl\|CDD\|234567	PRK00005, fmt, methionyl-tRNA formyltransferase; Reviewed.	2.64233e-142
NZ_CP029149.1\|WP_120489175.1\|1713150_1714230_-\|PASTA-domain-containing-protein	gnl\|CDD\|275384	sd00037, PASTA, PASTA domain. PASTA domain is found at the C-termini of several penicillin-binding proteins (PBPs) and bacterial serine/threonine kinases. It is a small globular domain consisting of 3 beta-sheets and an alpha-helix. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.	2.28656e-16
NZ_CP029149.1\|WP_160224503.1\|1709525_1710980_+\|HAMP-domain-containing-histidine-kinase	gnl\|CDD\|223715	COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms].	3.19347e-36
NZ_CP029149.1\|WP_160224728.1\|1711974_1713042_-\|RluA-family-pseudouridine-synthase	gnl\|CDD\|223638	COG0564, RluA, Pseudouridylate synthases, 23S RNA-specific [Translation, ribosomal structure and biogenesis].	4.73774e-109
NZ_CP029149.1\|WP_160224505.1\|1717650_1719081_-\|cation:dicarboxylase-symporter-family-transporter	gnl\|CDD\|234968	PRK01663, PRK01663, C4-dicarboxylate transporter DctA; Reviewed.	1.54585e-122
NZ_CP029149.1\|WP_160224497.1\|1699690_1701193_+\|GH3-auxin-responsive-promoter-family-protein	gnl\|CDD\|377019	pfam03321, GH3, GH3 auxin-responsive promoter.	5.29918e-95
NZ_CP029149.1\|WP_120489180.1\|1708931_1709516_+\|riboflavin-synthase	gnl\|CDD\|236455	PRK09289, PRK09289, riboflavin synthase.	7.28908e-92
NZ_CP029149.1\|WP_120489174.1\|1714347_1715328_+\|D-alanine--D-alanine-ligase	gnl\|CDD\|234993	PRK01966, ddl, D-alanine--D-alanine ligase.	8.95609e-128
NZ_CP029149.1\|WP_120489173.1\|1715337_1715796_+\|pantetheine-phosphate-adenylyltransferase	gnl\|CDD\|234674	PRK00168, coaD, phosphopantetheine adenylyltransferase; Provisional.	4.2327e-84
NZ_CP029149.1\|WP_120489168.1\|1719633_1720668_-\|DNA-polymerase-III-subunit-delta	gnl\|CDD\|273455	TIGR01128, DNA_polymerase_III_subunit_delta, DNA polymerase III, delta subunit. DNA polymerase III delta (holA) and delta prime (holB) subunits are distinct proteins encoded by separate genes. The delta prime subunit (holB) exhibits sequence homology to the tau and gamma subunits (dnaX), but the delta subunit (holA) does not demonstrate this same homology with dnaX. The delta, delta prime, gamma, chi and psi subunits form the gamma complex subassembly of DNA polymerase III holoenzyme, which couples ATP to assemble the ring-shaped beta subunit around DNA forming a DNA sliding clamp. [DNA metabolism, DNA replication, recombination, and repair].	7.47894e-40
NZ_CP029149.1\|WP_160224729.1\|1716912_1717611_-\|SAM-dependent-methyltransferase	gnl\|CDD\|381176	cd11649, RsmI_like, uncharacterized subfamily of the tetrapyrrole methylase family similar to Ribosomal RNA small subunit methyltransferase I (RsmI). RsmI, also known as rRNA (cytidine-2'-O-)-methyltransferase, is an S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent methyltransferase responsible for the 2'-O-methylation of cytidine 1402 (C1402) at the P site of bacterial 16S rRNA. Another S-AdoMet-dependent methyltransferase, RsmH (not included in this family), is responsible for N4-methylation at C1402. These methylation reactions may occur at a late step during 30S assembly in the cell. The dimethyl modification is believed to be conserved in bacteria, may play a role in fine-tuning the shape and functions of the P-site to increase the translation fidelity, and has been shown for Staphylococcus aureus, to contribute to virulence in host animals by conferring resistance to oxidative stress.	4.31754e-128
NZ_CP029149.1\|WP_160224504.1\|1716030_1716867_-\|RNA-binding-protein	gnl\|CDD\|225543	COG2996, COG2996, Predicted RNA-bindining protein (contains S1 and HTH domains) [General function prediction only].	7.33427e-58
NZ_CP029149.1\|WP_120489167.1\|1720674_1721118_+\|type-I-restriction-enzyme-HsdR-N-terminal-domain-containing-protein	gnl\|CDD\|372640	pfam13588, HSDR_N_2, Type I restriction enzyme R protein N-terminus (HSDR_N). This family consists of a number of N terminal regions found in type I restriction enzyme R (HSDR) proteins. Restriction and modification (R/M) systems are found in a wide variety of prokaryotes and are thought to protect the host bacterium from the uptake of foreign DNA. Type I restriction and modification systems are encoded by three genes: hsdR, hsdM, and hsdS. The three polypeptides, HsdR, HsdM, and HsdS, often assemble to give an enzyme (R2M2S1) that modifies hemimethylated DNA and restricts unmethylated DNA.	2.71442e-35
NZ_CP029149.1\|WP_120489187.1\|1701235_1701886_-\|uracil-phosphoribosyltransferase	gnl\|CDD\|234653	PRK00129, upp, uracil phosphoribosyltransferase; Reviewed.	1.54233e-79

>NZ_CP029149.1|WP_160224503.1|1709525_1710980_+|HAMP-domain-containing-histidine-kinase
MYTYKGLNLSLRNKVFWGFIFICFLSMAGTTLISYYILRNNSIQLSQTDQQNKADAMMAALDYSISHSEVDTRDLPKVLENAIYEIADINKHDLIIYDLQGNYLLSNKEKDLVPQKKVDQKIIHRLLQNQYRVDEQSYDEALEANLFSSYILLKNNVLKPIAIVYLPYYHSDSVYLSVLERYTKYIIFLNFIVILISIAVSWVISNNVSQTIRKFSDMIAKITLFGENMNPIRYYPNDELSSLVNSYNKMLLQIQYQKDRLSHTAKEGAWREMAKQVAHEVKNPLTPMKLSIQNFERKFNPEDPKIYDRVKNLCTTLISQIDLITAVADAFSQFETLPEKNNEVFNLKDEVMNIVQIFHEDDIKISSNRSDILINMDKIYLNRIIVNLITNAKQAKSDDRALRIHIKIEQINRKVKISVQDNGIGIAEDMYERIFEPNFTSKSSGKGLGLSMVKKMVTDYQGEISLRSEIGVGTSFIITLPASV
>NZ_CP029149.1|WP_120489180.1|1708931_1709516_+|riboflavin-synthase
MFTGIIEAMGRVEQIEKKGTNINFVLSSPFTSELKIDQSVAHNGCCLTIVDIAGDRYTVNAIDETLEKTNLGSWQVGSLINLERCMQMGGRLDGHIVQGHIDRTGVVAGIENKDGSYFVSISYDESREYTTVAQGSITVNGVSLTVAQSGSHSFSVALIPYTWEHTNLHLLKIGDSVNLEFDIIGKYVAKLINK
>NZ_CP029149.1|WP_120489181.1|1707603_1708680_-|4-hydroxythreonine-4-phosphate-dehydrogenase-PdxA
MSKTQKIRVGISIGDFNGIGPEVIMKCLKDKSITEFFTPVIFGSGKLFTSQKNIFKININFNYILKANQAQDGKLNMVNLWKDEVSVQLGTPTEESTKMAIDSLEAATEALKQGEIDVLVTAPINKDEMIKYGFKHAGHTGFLEEKLGAKGLMFLVTDSLKVAVSTHHIPITEVAQNISKEKIVEQVRLLNKTMIEDFCIQKPKIAILGLNPHAGDGGAIGKEEIDIINPAIKQLWNEGILAFGAFPADSFFQPEKYQKFDAVLAMYHDQGLAPFKTLAYEEGVNYTAGLPFVRTSPDHGTAYDIAGQNKADEHSFMEAIFTAIKIYKNRMEYQELIANQLKKSNIKDNGVDEDLPEA
>NZ_CP029149.1|WP_160224502.1|1707107_1707470_-|hypothetical-protein
MKTLVTFTFSIIILLVSTPSGFLMVDYHCNKNFYETHCINKKTPKSDCHGKCELRKNSKIKELSTNSTISFPEFNIISPEYISLSIQREIPLGDKKIADAQEHNSITSLFYDIPYPPPEV
>NZ_CP029149.1|WP_160224501.1|1705679_1706975_-|T9SS-type-A-sorting-domain-containing-protein
MNKVFLLFSILLSSLYFSQGGDVPASERAELERIYNENNGEKWPKKEKWNSVSPVEEWEGISVVTNEKGEKHIETINLTSNQLTGVFSLANLPELKKIFLSSNQISGISLDKTLEKLSYLMIDDNNLEELHLENFQLLEQINVYSNANLATLSLNNLPKLKNIQAYSCKLNNVSLSSLGALETLSLHGNQISSIDLSPFTTLTHLYLAKNTFTTLNIRGLSQLKFLDIQENLKLTTLETGEHPELINFYASKSNELKGYIDLGKSAKLKIFHALHTKVEAVNLKNGNNKWMASKNSVLISDKVKCIAVDDPKAARNPSTPRNNPYKSKNWDIIWATGYTRENGFQEDCKDALNADEVQVQKRDFKLTNPVKEVLWVQGLEDIKTIEIYSPNAQLIKTISGNKANVSSLAKGLYFIKIYTTKGVLTSKIIKE
>NZ_CP029149.1|WP_160224500.1|1704527_1705676_-|T9SS-type-A-sorting-domain-containing-protein
MNKLFFILSLVFCLSLSAQDVPENERNILISFYNQTNGNDWADHTNWATNEPVESWHGITVEEIEGKKHITKVHLPANNLTGELALGDLPHLKILHLRKNKLTKVAINNFPKLEILQIDYNATLTEATFNSLPELLELSLNEDRLTQISVHPKELPKIQELHLRGNHFKTAFFENLEHLKWLFINKCPYLESLSISNLPALERLYVNQDFKLAGYLDLSSFSKLKAFIAAYTSLSVVNLKNGNNINAETYEDAISIYHDSKNLVKCVAVDNPDAAMKNELPYKNWKIRWVDLKPNYRADCSDYMASDEVKTKSSFKISNPVKDTLWIQGVDGLKSIEIYSSTGQLVKTILGNQGDVSSLPKGVYFLKINTPSESLTAKIIKQ
>NZ_CP029149.1|WP_160224499.1|1703381_1704329_-|methionyl-tRNA-formyltransferase
MSALRVVFFGTPDFAAESLRAIHQSAHEVVGVVTVADKASGRGQKVNQSPVKRFAVEHHLPLFQPEKLRDNEFLESIRALNADIFVVVAFRMMPKILWEMPKLGTFNLHASLLPDYRGAAPINYAIINGESETGVTTFFINEKIDEGNLLLQAKTAIGDDENAGSLHDRLMEIGSKLVVETLDRLSEGCITERPQPQVEHPKNAFKIFKEDTRIYWQQPSQAVHNFIRGMSPYPCAFTTLSINGESKGLKIFSGKYELLPHKREAGKIELSKSELRIFTQDGIYSPEEVQLEGKKRMSIKDFLNGFQSLEGIQLG
>NZ_CP029149.1|WP_160224498.1|1701963_1703274_-|ribosome-biogenesis-GTPase-Der
MSNIVAIVGRPNVGKSTLFNRLLERREAIVDSTAGVTRDRHYGKSEWCGVEFTVIDTGGYDVGSDDIFEEEIRKQVQLAIDEATSVIFILNVEEGLTDTDHEIYHLLRKANKKVYIVVNKVDSSKEELPATEFYQLGIDGYYTISSATGSGTGDLLDDIIKDFPTKEYKDPFEGLPKITIAGRPNVGKSTLTNALLDNERNIVTHIAGTTRDSIQSLYNKFGHEFVLVDTAGMRRKNRVSEDLEFYSVMRSVRAIENSDVVIIMVDASLGWESQDMNIFSIAQRNRKGIVILVNKWDLVEDKKANTMKEFEAGIRHKIGQFSDVPILFISALTKQRILKAVDTAMEVYENRKKKIKTSKLNEIMLPIFENTPPPAIKGKYIKIKYCVQLPTPSPQFVFFCNLPQYIKEPYKRFTENQLRKEFGFTGVPIEVYFRQK
>NZ_CP029149.1|WP_120489187.1|1701235_1701886_-|uracil-phosphoribosyltransferase
MTTILSENFSLVNSWINELRNVEVQQDRMKFRRNLERIGEIAAFEISKHLEQKEIEITTPLDKIKVREIAVQPVITTILRAGVPLFQGVLNYFDKADCGFVAAYRKHDANDYFSIKQDYLTCPNIEGRPLIVADPMLATGASLIEALKDLLTNGKPSQIHIVAAIASKIGVETVQKAYPEAHIWVGALDENLTPKGYITPGLGDAGDLSYGEKLQR
>NZ_CP029149.1|WP_160224497.1|1699690_1701193_+|GH3-auxin-responsive-promoter-family-protein
MINFLKKKLALIFAKREVAKSEHFKHNAASDQQKLLLSLVRNAEKTLFGRAYGFSEIHSVEDFQKRVPITNYEALLPFIKKLKHGDRNILWTDVPEYFAKTSGTTSGSKYIPISKEGINDQINAARLALLHYIAQKGNANFITGKMIFLQGSPQLSEVGGIKTGRLSGIVAHHIPKYLQKNRLPKYETNCIEDWETKVDQIVKETETENMTLISGIPPWLIMYFEKLIAKNGKKIKELFPNLQIIVTGGVNYEPYREKMEELLGGKVDIIQTFPASEGFFAFQDDYTKDGLLLLTNHGIFYEFIALEDYGKPDAKRLTLAEIELDKDYALIISTNSGLWAYSIGDVVRFISKNPYKILVSGRTKHYTSAFGEHIIAFEAEEALKATVMAFPAQITEFHLAPQVNPASSLPYHEWFIEFEKEPESLDAFKAQLDREMRKRNPYYDDLISGSVLQPLVITRLKKNAFNDYAKAEGKLGGQNKIPRLANDRKIADKLSSYVLK
>NZ_CP029149.1|WP_160224728.1|1711974_1713042_-|RluA-family-pseudouridine-synthase
MEHPNEDLFEEDFSTTDTSSDDENSGLFEHLSITVDKKQEPLRIDKFLLIYRQNSSRNKISQTCRAGNVLVNGQPVKQNYRVKPGDEISVLLAHPPRENVIIPQNIPINIVYEDDDVLVIDKEAGMVVHPGFGNWDGTLVNAVAYHFEQNGLKTDLDRIGLVHRIDKDTSGLLVIAKNEYALSHLAKQFFDRKTKRLYWAFVWGNLEDDQGTIRGNIGRHLKNRMQMAVYEDGSHGKHAVTHYKVLERFRYMTWVECKLETGRTHQIRAHFRHIGHTLFNDERYEGNVILRGINLPKYKQFVQNVFEILPRHALHAHTLGFIHPTTKEEMYFESPMPHDMQSAIDKWRNYLSAQQ
>NZ_CP029149.1|WP_120489175.1|1713150_1714230_-|PASTA-domain-containing-protein
MLKSFFNWKVLLNIVIAMVVFIGLIFFTFRWLEHHTNHGQEIPVPNIINMQITDAIKTLEDAGLQYKVDSGEFQPQYKPLQVLQIWPAPGSRVKSNREIEIRINPKTWAKVTIPDILDRYKGLAFRQLEQVGLKIGDTIYEPSIQRDAVIRMQLDGKVLKPGDQVARFTPIDLVIGTGPKRNVPIPNLIGLTVEEAEMIIGRHLFEIGLVEYEDGKGDKTDIIYFQDPAGGALRDQGMQIDLWASKKVPSEMGDKISQLNSIYRTRVENIPSDDGYYINDNAFGTEHLSSPKPIDSPKIKPQPEKPKAETPKPKKEDNPQPKKENKPETSKPKDNQPKKTEEKPKPKDEKPKVKKVVVE
>NZ_CP029149.1|WP_120489174.1|1714347_1715328_+|D-alanine--D-alanine-ligase
MAKKNVAVVMGGYSDEYKVSLRSGELIFESLDRNLYNVFKVVILKDEWYFLDDDGSKLPINKADFSVSRGEKILKFDVCFNTIHGKPGENGELQAYWDTIGQRYTGCNFYQSALTFNKKDTLAVLSKYGIPSAKSIYIRKGEKVDAEKIISELSLPLFVKPNQSGSSLGISKVKDISDFDKALDFAFAEDDEVLIESFLDGTEVSVGVIDYKGKTTVLGITEIVPKNEFFDYEAKYEGASEEITPARLDDETRQKVEDIAKRAYESLGMSGFSRSEYIIMNGTPYLLEMNTNPGFSPASILPQQARHYGMSITDLCGNEVEKALNK
>NZ_CP029149.1|WP_120489173.1|1715337_1715796_+|pantetheine-phosphate-adenylyltransferase
MKIAVFPGSFDPITLGHYDIIERAVPLFDKLIIAIGQNSKKNYMFPLEKRIEFIQKSVEHFPNVEVDYYEGLTVDYCAKKNAQYILRGLRNPADFEFEKAITHTNRTISHKKLETVFLLTSSGKSFISSSIVREIIAHNGDYSLLVPEAVTL
>NZ_CP029149.1|WP_160224504.1|1716030_1716867_-|RNA-binding-protein
MQAGKTQTLTITEKTNQGFYLSDVNNETVFIANIFSENHWKKGDEVEVFIYQEDGILKATNEKPYAEVGEFAVMKCVQTLPSGAFLDWGIIKDIFVPYKEQKGKMVEGKRYLVFVYEDEATGLITATAKFKRNPSYSHLPLKKGEKVSLIVMNESELGWNVIINQKYIGLVYASEVYTPLYPLSEIIGYIKTLREDGKIDVSLQPQGFENIEIYKEYILQKLEENYGLLHLSDKSSPEEIKSVVQMSKKNFKKAIGSLYKEQKIQIFEDKITIVNDKR
>NZ_CP029149.1|WP_160224729.1|1716912_1717611_-|SAM-dependent-methyltransferase
MLFLIPAYLSDESPQAYFAPIIKEYILKTDYFFVENEKTARKVIKFFAPEKKQADLKLFLLDKYSETEDLKEAQQLMKQGQDFGLLSEAGLPCIADPGNIMVSWAHRNGIKVIPVNGPSSIILALIGSGFNGQEFTFHGYLPIDKSQKKAKIQQLEQQVQRTGYTQIFMETPYRNNQLFDDLTKYLSPSSKLCIAANINHPAEEFIKTLSIRDWKNHKPELHKIPTVFVLGR
>NZ_CP029149.1|WP_160224505.1|1717650_1719081_-|cation:dicarboxylase-symporter-family-transporter
MKHLKIFRLIALLSVITASIAHGIHFLSPISDEILKAAHLFLGIGAILYGISRKHLTTWIMVSIILGVLVGSDAPSIAIALQPLSQGFIKVIKTIVGPILIATLVYGIAGHSDLKQVGRMAWKSLVYFYSLTTIALFIGLAAINISQAGAGVDASKIPQYELPSASSAKEKDLKALEHIPENDQWIYKTTSFFRDIFPENIIKSVYENQVLQIVVFSVIFGIGLAKLPEEKKRPIVDFMDSLAETMFKYTHIVMYFAPMGVGAAMAYTVGHMGVDILKYLFMLLFTLYAALIAFILLILLPIALYFKIPIRKFIQAIKEPVSIAFATTSSDAALPTVMQNMENFGVPRKIVSFVVPTGYSFNLDGTTLYLSLASIFVAQAAGIDLSFGQQLLICLTLIVTSKGVAAIPRASLIILISTADQFGLPTFIIAAILGIDELMDMGRTSVNVIGNCLASVVIAKWEGEFDDAKALAFEEE
>NZ_CP029149.1|WP_160224506.1|1719162_1719621_-|BON-domain-containing-protein
MKRLIRINLISILALMLVGCDANSDEVLQQQAEQIISAYPNASVEVKDGVLTLKGNFDTSKDKAEALQKLNKIKDTQTVKDEAASLEDLIKDTSISPEDLQKVIDLAKDFPSIQVEVVDGKLTLTGKASSTQDKIIRRSLPTLDIDYNYTVQ
>NZ_CP029149.1|WP_120489168.1|1719633_1720668_-|DNA-polymerase-III-subunit-delta
MKELESLVKNIKNKEILPIYFLHGAEPYFIDQLVKVIEDEVLSEDERDFNQTVVYGKDTSYPEVLSLARQFPMMGERQVIIVKEAQDLRLTETETEALIQYAQNPIPSTVLVFAHKNKKLDGKKKKLNAALKPYLFLSEEVRDYELPKLIQQELQKMGIKTAPNISNLLAEYMGNDLSRIFNELNKVKIILKDGEVLDEKLVERYIGISKEYNVFELQNAIALKDVTKAFKIAYFMGKNEKENPIISIVSVLFSFFSKVIIYHTLADKSKASVATALGINPFFVKDYQASAGLYPLKYATRIITLLREIDMKSKGLGANQTSDGELLKELVYKIINIDKIKVKV
>NZ_CP029149.1|WP_120489167.1|1720674_1721118_+|type-I-restriction-enzyme-HsdR-N-terminal-domain-containing-protein
MELPVLNFKTKFDFQIKRDKDKFFIYDVVRKAWLLLTPEEWVRQHWVHFFITEKKYSPSALITEKKVEVNGTPKRIDLLITEKTLPKILIECKAPHIKLSEKTFEQVARYNSTIGAEQIILSNGLHHISAQYDSHTQQYTIGKQAFG

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Crispr_ID: NZ_CP029149_11

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP029149_11

1899133-1899222

Orphan

Consensus_repeat	Method
TTAAAATATTTAATTAAAAAACAC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP029149_11

>merge|NZ_CP029149|11|1899133-1899222|CRISPRCasFinder
TTAAAATATTTAATTAAAAAACACTTCTCCCTCCCTTCAATTTAAGTGCCAATGTCTAAAAATTAGTTAAAATATTTAATTAAAAAACCG

>NZ_CP029149|11|10|1899133-1899222|CRISPRCasFinder
TTAAAATATTTAATTAAAAAACAC	TTCTCCCTCCCTTCAATTTAAGTGCCAATGTCTAAAAATTAG
TTAAAATATTTAATTAAAAAACCG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP029149.1\|WP_120489018.1\|1911077_1912451_+\|signal-recognition-particle-protein	unknown	unknown	gnl\|CDD\|236780
NZ_CP029149.1\|WP_160224611.1\|1906376_1908191_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|226664
NZ_CP029149.1\|WP_120489022.1\|1904290_1904872_-\|DUF479-domain-containing-protein	unknown	unknown	gnl\|CDD\|225666
NZ_CP029149.1\|WP_120489021.1\|1904948_1906292_-\|DNA-repair-protein-RadA	unknown	unknown	gnl\|CDD\|236994
NZ_CP029149.1\|WP_160224609.1\|1900604_1901855_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_160224602.1\|1886002_1887745_-\|T9SS-type-A-sorting-domain-containing-protein	unknown	unknown	gnl\|CDD\|275036
NZ_CP029149.1\|WP_120489027.1\|1892460_1894236_+\|30S-ribosomal-protein-S1	unknown	unknown	gnl\|CDD\|235775
NZ_CP029149.1\|WP_160224734.1\|1884313_1885882_+\|ribonuclease-Y	unknown	unknown	gnl\|CDD\|237177
NZ_CP029149.1\|WP_160224610.1\|1902123_1904262_+\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|350795
NZ_CP029149.1\|WP_160224608.1\|1899356_1900442_-\|RNA-directed-DNA-polymerase	RT	pfam00078_RT_CAS-I:CAS-III	gnl\|CDD\|239569
NZ_CP029149.1\|WP_160224735.1\|1897037_1899092_-\|OmpA-family-protein	unknown	unknown	gnl\|CDD\|143586
NZ_CP029149.1\|WP_120489020.1\|1908317_1909790_-\|amidophosphoribosyltransferase	unknown	unknown	gnl\|CDD\|223112
NZ_CP029149.1\|WP_160224607.1\|1895998_1896871_-\|4-hydroxy-tetrahydrodipicolinate-synthase	unknown	unknown	gnl\|CDD\|235107
NZ_CP029149.1\|WP_160224606.1\|1894985_1895939_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|366092
NZ_CP029149.1\|WP_160224603.1\|1887908_1889651_-\|T9SS-type-A-sorting-domain-containing-protein	unknown	unknown	gnl\|CDD\|275036
NZ_CP029149.1\|WP_120489701.1\|1894553_1894976_+\|hotdog-fold-thioesterase	unknown	unknown	gnl\|CDD\|161843
NZ_CP029149.1\|WP_160224613.1\|1912465_1914604_+\|OmpA-family-protein	unknown	unknown	gnl\|CDD\|143586
NZ_CP029149.1\|WP_160224612.1\|1909805_1910525_-\|phosphoribosylaminoimidazolesuccinocarboxamide-synthase	unknown	unknown	gnl\|CDD\|181800
NZ_CP029149.1\|WP_160224605.1\|1890515_1892288_+\|aminopeptidase-P-family-protein	unknown	unknown	gnl\|CDD\|238518
NZ_CP029149.1\|WP_160224604.1\|1889816_1890482_+\|monofunctional-biosynthetic-peptidoglycan-transglycosylase	unknown	unknown	gnl\|CDD\|234603

Protein	Function_ID	Function_description	E-value
NZ_CP029149.1\|WP_120489018.1\|1911077_1912451_+\|signal-recognition-particle-protein	gnl\|CDD\|236780	PRK10867, PRK10867, signal recognition particle protein; Provisional.	0
NZ_CP029149.1\|WP_160224611.1\|1906376_1908191_+\|TonB-dependent-receptor	gnl\|CDD\|226664	COG4206, BtuB, Outer membrane cobalamin receptor protein [Coenzyme metabolism].	2.39623e-47
NZ_CP029149.1\|WP_120489022.1\|1904290_1904872_-\|DUF479-domain-containing-protein	gnl\|CDD\|225666	COG3124, COG3124, Uncharacterized protein conserved in bacteria [Function unknown].	5.82259e-20
NZ_CP029149.1\|WP_120489021.1\|1904948_1906292_-\|DNA-repair-protein-RadA	gnl\|CDD\|236994	PRK11823, PRK11823, DNA repair protein RadA; Provisional.	0
NZ_CP029149.1\|WP_160224602.1\|1886002_1887745_-\|T9SS-type-A-sorting-domain-containing-protein	gnl\|CDD\|275036	TIGR04183, hypothetical_protein, Por secretion system C-terminal sorting domain. Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.	1.80883e-09
NZ_CP029149.1\|WP_120489027.1\|1892460_1894236_+\|30S-ribosomal-protein-S1	gnl\|CDD\|235775	PRK06299, rpsA, 30S ribosomal protein S1; Reviewed.	0
NZ_CP029149.1\|WP_160224734.1\|1884313_1885882_+\|ribonuclease-Y	gnl\|CDD\|237177	PRK12704, PRK12704, phosphodiesterase; Provisional.	0
NZ_CP029149.1\|WP_160224610.1\|1902123_1904262_+\|AAA-family-ATPase	gnl\|CDD\|350795	cd18037, DEXSc_Pif1_like, DEAD-box helicase domain of Pif1. Pif1 and other members of this family are RecD-like helicases involved in maintaining genome stability through unwinding double-stranded DNAs (dsDNAs), DNA/RNA hybrids, and G quadruplex (G4) structures. The members of Pif1 helicase subfamily studied so far all appear to contribute to telomere maintenance. Pif1 is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.	2.94266e-48
NZ_CP029149.1\|WP_160224608.1\|1899356_1900442_-\|RNA-directed-DNA-polymerase	gnl\|CDD\|239569	cd03487, RT_Bac_retron_II, RT_Bac_retron_II: Reverse transcriptases (RTs) in bacterial retrotransposons or retrons. The polymerase reaction of this enzyme leads to the production of a unique RNA-DNA complex called msDNA (multicopy single-stranded (ss)DNA) in which a small ssDNA branches out from a small ssRNA molecule via a 2'-5'phosphodiester linkage. Bacterial retron RTs produce cDNA corresponding to only a small portion of the retron genome.	5.66905e-73
NZ_CP029149.1\|WP_160224735.1\|1897037_1899092_-\|OmpA-family-protein	gnl\|CDD\|143586	cd07185, OmpA_C-like, Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA. OmpA-like domains (named after the C-terminal domain of Escherichia coli OmpA protein) have been shown to non-covalently associate with peptidoglycan, a network of glycan chains composed of disaccharides, which are crosslinked via short peptide bridges. Well-studied members of this family include the Escherichia coli outer membrane protein OmpA, the Escherichia coli lipoprotein PAL, Neisseria meningitdis RmpM, which interact with the outer membrane, as well as the Escherichia coli motor protein MotB, and the Vibrio flagellar motor proteins PomB and MotY, which interact with the inner membrane.	3.93794e-31
NZ_CP029149.1\|WP_120489020.1\|1908317_1909790_-\|amidophosphoribosyltransferase	gnl\|CDD\|223112	COG0034, PurF, Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism].	0
NZ_CP029149.1\|WP_160224607.1\|1895998_1896871_-\|4-hydroxy-tetrahydrodipicolinate-synthase	gnl\|CDD\|235107	PRK03170, PRK03170, dihydrodipicolinate synthase; Provisional.	1.66526e-124
NZ_CP029149.1\|WP_160224606.1\|1894985_1895939_+\|hypothetical-protein	gnl\|CDD\|366092	pfam00425, Chorismate_bind, chorismate binding enzyme. This family includes the catalytic regions of the chorismate binding enzymes anthranilate synthase, isochorismate synthase, aminodeoxychorismate synthase and para-aminobenzoate synthase.	6.0088e-51
NZ_CP029149.1\|WP_160224603.1\|1887908_1889651_-\|T9SS-type-A-sorting-domain-containing-protein	gnl\|CDD\|275036	TIGR04183, hypothetical_protein, Por secretion system C-terminal sorting domain. Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.	7.07953e-09
NZ_CP029149.1\|WP_120489701.1\|1894553_1894976_+\|hotdog-fold-thioesterase	gnl\|CDD\|161843	TIGR00369, Putative_esterase, uncharacterized domain 1. Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown.	2.43002e-35
NZ_CP029149.1\|WP_160224613.1\|1912465_1914604_+\|OmpA-family-protein	gnl\|CDD\|143586	cd07185, OmpA_C-like, Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA. OmpA-like domains (named after the C-terminal domain of Escherichia coli OmpA protein) have been shown to non-covalently associate with peptidoglycan, a network of glycan chains composed of disaccharides, which are crosslinked via short peptide bridges. Well-studied members of this family include the Escherichia coli outer membrane protein OmpA, the Escherichia coli lipoprotein PAL, Neisseria meningitdis RmpM, which interact with the outer membrane, as well as the Escherichia coli motor protein MotB, and the Vibrio flagellar motor proteins PomB and MotY, which interact with the inner membrane.	1.74602e-31
NZ_CP029149.1\|WP_160224612.1\|1909805_1910525_-\|phosphoribosylaminoimidazolesuccinocarboxamide-synthase	gnl\|CDD\|181800	PRK09362, PRK09362, phosphoribosylaminoimidazole-succinocarboxamide synthase; Reviewed.	7.18848e-142
NZ_CP029149.1\|WP_160224605.1\|1890515_1892288_+\|aminopeptidase-P-family-protein	gnl\|CDD\|238518	cd01085, APP, X-Prolyl Aminopeptidase 2. E.C. 3.4.11.9. Also known as X-Pro aminopeptidase, proline aminopeptidase, aminopeptidase P, and aminoacylproline aminopeptidase. Catalyses release of any N-terminal amino acid, including proline, that is linked with proline, even from a dipeptide or tripeptide.	1.5915e-115
NZ_CP029149.1\|WP_160224604.1\|1889816_1890482_+\|monofunctional-biosynthetic-peptidoglycan-transglycosylase	gnl\|CDD\|234603	PRK00056, mtgA, monofunctional biosynthetic peptidoglycan transglycosylase; Provisional.	1.08967e-98

>NZ_CP029149.1|WP_160224735.1|1897037_1899092_-|OmpA-family-protein
MLSAHQLSAQKYLGLSNSNYSGVYGSQYNPAKLAGNKYVFSMNFLSVNGLVDNDLYKFSSIEAFRNMNLNNFGNIASKENQNLVSTLYVGEVLGPSLQFTVNDRLGFGVSSRLRTFGQSDNLTSDFVNIINSNRGTTSATGLLSNSAGSFTASSLSDLGVSGAYSVINNDKFRLTLGAGVKLYRGLKLNNFKSNNYNLDYNYNSTTNTSTFDVNSANWEFYTNVPSGGSISNPLGSIATSIGDMYDFSSGSTAVGGNFGAEAVFKGSNSEKPYAFKLGAAIHDLGSISYKDVTKYTVKGNGAGINPLEFNLADVNSTVNYLQSKGLTVTKTANQEFKSDLPTHVTAYADYAFTKKFFVSANALVNLAEKGANSVHYNSSVSLAPRWESKWFDVSVPLTYQLDNSDFKPGLAFRVGPLSVGSDDIKVLFTDAKGANVYAGLNFSLGRKKTAEPEVVPAEPVREVDSDGDGIVDNKDRCPYEAGPAENQGCPWPDTDGDGVLDKDDKCPTVPGLASNQGCPKAHETVAKEVTLALKDILFNFGKATINPESNKKLDTAAKIIKDSKGGTYLLVGHTDKKGNEAYNLKLSRERAVAVVQALEERGVPADQLKSKGVGSKEATTPATASDAERQKDRRVEVLHITGSEWEALSKSDVPVAKKKVATSAKGKASAKKAPVRKAAPKKKK
>NZ_CP029149.1|WP_160224607.1|1895998_1896871_-|4-hydroxy-tetrahydrodipicolinate-synthase
MKSLKGLGVALVTPFNEDLSVDFSSLTRLVEYNIANGCNFLVVLGTTAEAATLSKEEKKQVTEHIIKVNNGRLPLVLGIGGNNTAEVKKQIEETDLSAFEAVLSVSPYYNKPNQEGIYQHYRALAETGKQIIIYNVPGRTGQNVEASTTLRLAKDFTNLSIIKEAAPNIAQYFDILRKKPAGFSLLSGDDEFTLPVTLAGGSGVISVIGQAYPKQFSDMLKLAFERRVDDAYAIHNSLVEITRLIFAEGNPVGIKTVLAEMGLIKNVLRLPLVKASKDLEERIKAEMKNL
>NZ_CP029149.1|WP_160224606.1|1894985_1895939_+|hypothetical-protein
MLVFRMPFEARFLSTDLFGEESLVSFSSFDLSETLSFKGNIKEIPLDEVGQLPFILSENNDEAGESREEYFDKLSQTIQVINAHQLPKLVIARRKIININEVDIPQTLKNLAEFYPSAFVYAFQHKGGVWMGAFSEVLGKYDKKSHLFETMSLAGTLPVEESWTKKEIEEQKPVSSYIHNILSRYAQEVRTSETYDFVSGNIKHLRTDFSIKIEESSLDDVINDLHPTPAVCGIPKDFCKEKIREIEGFDREFYAGYSKVEIDEKIYYFVNLRCGKFYKNSAVLFVGGGITRMSSPEKEWRETELKSQALGRNITTL
>NZ_CP029149.1|WP_120489701.1|1894553_1894976_+|hotdog-fold-thioesterase
MDEENKKEILERLNNWGTETLAKTLGIVFTDVSEDSLSATMPVNPKIHQPYGILHGGASVALAETLGSCLSFLSIDPEKFYPVGTNINSNHLRPKKEGTVTGRATFIRKGRTMHISQIEIRDEQGKLINHTTMTNTILSH
>NZ_CP029149.1|WP_120489027.1|1892460_1894236_+|30S-ribosomal-protein-S1
MSELTNKEEVLMNQNVAPEQFDWDSFESGLDAEARKEKSDLEEIYKGSLNDLEDNDVLVGKVVRLTDKEAIVDINFKSEGVISLNEFRYNAGLKVGDEVEVMVDRREDKTGQLQLSHKKARTLRAWDKVNELHQSGEVVNGFVKSRTKGGMIVDVHGIEAFLPGSQIDVKPIKDYDQFVGKTMEFKVVKINPEFKNVVVSHKALIEADIEDQKKEIIAQLEKGQVLEGTVKNITSYGVFIDLGGVDGLIHITDLSWSRVNHPTEILEDGQTVKVVILDFDDEKTRIQLGMKQLEPHPWEALDANLKVGDKVKGKVVVLADYGAFVEIAPGVEGLIHVSEMSWSTHLRSAGDFVKVGDEVEAEILTLDRDERKISLGIKQLTNDPWADIEAKYPVGSKHNGAVRNFTNFGVFVELEEGIDGLVYISDLSWTKKIKHPSEFCSVGDKMDVVVLELDKEARRISLGHKQLTENPWDVFETKYAEGTVHSGVALDVFDKGAQVQFEDAEVEAFCPSRLLEKEDGSKIKKGETADFKVIEFNKEFKRVVVSHTGIFREEERKNVKDAAAKSSSEEKTTLGDIDALAELKKKMEEGK
>NZ_CP029149.1|WP_160224605.1|1890515_1892288_+|aminopeptidase-P-family-protein
MNTTEKISVLRTKMRDNNVDAFIVFSADPHMSEYLPHEWQERAWVSGFTGSAGFVVFTRDKAGLWTDGRYFTQAGVELKDTGITLMKDGVEGTPNYIDWILENIPQGGKVAVNALATSHANWEQISSKLQNGGASLIHLPLIDEIWSDRPSPSKNKVFTQPVERAGKSVQDKLSTIRAKVQEAGATAHIISSLDDVAWTLNLRGSDVNANPVFLGYIYLSLNDAVLFVDLEKLETDAKEQLDKSGVKAVSYHDFFHFLSGIDGEKILISPNTNQLVFEALKAKNTFIKAAVPGNLMKAQKNETELEGFRIAMEKDGVAMVKFLHWLTHNAGKIEMNEYSIGEKLTSLRAEQENFVGVSFDSIIGYKENGAIIHYSAKSEGSKEITNSGTILVDSGGQYLEGTTDITRTFALGNDVSQDFKINYTLVLKGMINLSMVKFPKGTRGVQLDAFARLPLWQAGKDYNHGTGHGVGSFMNVHEGPQNIRKDLNPVELMPGMVVSNEPGFYLVGEYGIRLENLIAVREVETTDFGVFYGFETLTICPFFKDVIIRELLSEEEIQWLNNYHKLCEEKLSKHLDGEVKDWFLQLVQPL
>NZ_CP029149.1|WP_160224604.1|1889816_1890482_+|monofunctional-biosynthetic-peptidoglycan-transglycosylase
MWKTLKRLILILILANILFIVWGRFFNPPITITQIGGYLDYGKLQREYIPYDEMGENIKKAVIASEDQNFFIHQGFDFKAIERAMKFNEKSTSGKMQGGSTISQQTAKNVFLWQGRSWLRKGLEAIYTFIIERVWTKEIILERYLNSIEMGQGVYGIEAAADYYFHKPAKNLTKSEAAWIAAVLPNPKKYDPKNPTKKLNKKHKWIMQQMNHISLSPNKGK
>NZ_CP029149.1|WP_160224603.1|1887908_1889651_-|T9SS-type-A-sorting-domain-containing-protein
MKKIYCSIGLLAFIGMKAQVFEEVTPSPFKNSYYSSIAVGDYNNDGYKDVFFAGALDTDNDNDVDTTINELYKNNNGVFELAQVIEDYPVHLSSVKFIDFDNDGLLDIIDTGLSYKNVVDYRHYRFKNNGSSFELVDNLPGKIYGNIDVFDFNHDGKMDYSLNGVRYVQGVGFTKYVDLYTNSKSGFTKEENWILGSQNGKMKAFDFNNDNELDAVVTGVDNKNNFSFFIYKNNGKKMELHSEQKGLISGDVTFADFNADGFLDIVVSGKDSNHDSHLIVLWNDGNGNFTESEIPNEGLEMASIDVGDLNNDGYYDFIIIGNAKDANSRYVPNINVFIYDPKGNNFSKFDDTDIYHLGSNGSIELVDYNNDNHLDIIATGFDWKLPDTPLFSKLFKNKETKPNEKPNPPKNLSATVKDDRVVFEWSGASDDKTPEKALRYEISVGSESGKSDIAKYEVTTPSWYLKKENLPNTIYWSIKSIDASKVLSVSSKEQMAYDLSVDDRDIKHKALYPNPVKDILNISTDAKVKSYKLTNMLGQTVKEGSLSGKEIDLSVLESGIYIIDIQLQNGENINQKIIKN
>NZ_CP029149.1|WP_160224602.1|1886002_1887745_-|T9SS-type-A-sorting-domain-containing-protein
MKKFYCSIGLLAFIGMKAQVFEEVTPSPFKNSYYSSIAVGDYNNDGYKDVFFAGALDTDGNGKVDTTINELYKNNNGVFELAQVIEDYPVHLSSVKFIDFDNDGLLDIIDTGLSYKNVVDYRHYRFKNNGTSFELVDNLPGKIFGNIDVFDFNHDGRMDYSLNGIRYIPGVGFTKYVDLYTNTKSGFTKQENWISGSQNGKMKAFDFNNDNELDAVVTGVDAKNKFSFYVYKNNGKTMEFHSEHIGLISGDVAFADFNADGFLDMVISGRNNKYTEQLVVLWNDGNGNFTESEILGEGIEMASIDVGDLNNDGYYDFIIIGNAKDANSHYVPNINVFIYNPKENKFSKFDDTDLYHLGSNGGIELVDYNNDNHLDIIATGFDWKLDDNPLFSKLFKNKETEPNQKPKPPKNLSATVKDDRVFFEWSGASDDKTPEKALRYEISVGSESGKSDIAKYQVTTPSWYLKKDALPNTIYWSIKSIDASKVLSDSSKEQVVSDLSVDDRDIKHNALYPNPVKDILNISTDAKVKSYRLTNMLGQTVQEGSLLGKEIDLSALESGVYIINIQLQNGENINQKIIKN
>NZ_CP029149.1|WP_160224734.1|1884313_1885882_+|ribonuclease-Y
MMIEIIAGIIGLIVGVAAGILFSRSSLNSKAKFMMEDARKNAENLVEKATVQAEAIKKEKQLQTKEKFLELKSQHDADIQAREKKIQEIEKRAKEKEQKLVDELSKTSKLEKDLEKQIYDYTKKHEIVEKKQAELNAITAQKVEILEKISNYSAEEARAELVESLKSEAKTRAQAHVQSIMEEAQMNAKNEARKIVIQTIQRIGAEQAIENSVSVFNIESDEVKGRIIGREGRNIRALEAATGVEIIVDDTPEAILLSCFDPVRREIARLSLHRLVTDGRIHPARIEEVVEKTRKHIEEEIIEVGKRTIIDLGIHGLHPELVKIVGRMKYRSSYGQNLLQHSREVANIAATMAAELGLNVKLAKRAGLLHDIGKVPEQESELPHALLGMQWAEKYGEHPEVLNAIGAHHDEIEMTSLLSPIVQVADAISGARPGARRQVLESYIQRLKDLEAAALSFDGVSSAYAIQAGRELRVIVESGKVNDEVAAQLSYDISEKIQNELTYPGQVKVTVIRETRAVNIAR
>NZ_CP029149.1|WP_160224608.1|1899356_1900442_-|RNA-directed-DNA-polymerase
MTSPSNKTIEDYSAEYQNEINAYQSVLNKNNLPVIYSLNHLCLMAEVNFEKIKIICDSNRQDSYKRFKLRKKRGGFRVIQTPQDELKYLQRWILENILNKKSSHNACKGFDPNTSIKLNAEKHLGQDGILKIDLLRFYDSINEKRVYGLFKSLGYHPNLSVSLAKICTIVPDNTFLCSFKKKERHLKQKIQRQSNLGVVPQGAPSSPKISNLIAISLDNRLQKLANKHDLNYTRYADDLTFSGKIEILSKIKKAIYRIIKEENLYPNYSKTKILKRGNPFFVTGLSVHNNIVTVPKKKKLEIEHHLHHCIKNGVQSHLITSKITNRNFKDWLLGNIAFVNSVEKELGEKYFKQFNEIQWPI
>NZ_CP029149.1|WP_160224609.1|1900604_1901855_-|hypothetical-protein
MTLNLEIDNTTLDILTTKLKVVSQLDILKWLSNFPKSEHKFALNILQNLTVYTIDDIENILNDSFSDLIKEIPGTNQVIVIPLGKFGKSGSMISYFFQKTSTSKKNKRIHLKSSLDNIEDISKPYSLVIIDDFIGTGSSFVSFFNEKILVHKEKFSEIYFIGIAGMDFGVKEVKKYVSVRIPISNIFKKAFSSEASYFGYRNYSKHREFCYKYGSKLVAPKKSKSEKDNVLGYGNSQSLVSFSYGTPNNTLPIIWANKEDWIPLIPRFSIDRISNSKNLRKSILHELSILREFGSDQLKETFFSFSIKRGKRHFSSVNKIDFSIYSIIKLSRRKYTSVSICQILGILHKDYEAIISECITKKIMNIDGSLTLLGLNLYNDAKKCIESRKRYAEKESQDYYKIREVKYLPKIFNGKS
>NZ_CP029149.1|WP_160224610.1|1902123_1904262_+|AAA-family-ATPase
MNQQESIFQLIEHTNRSIFLTGKAGTGKTTFLNNFVQKTRKKHIIVAPTGIAAINAGGVTIHSMFGLPLRTFVPTSERIDQNLANNIADLTHHFKYRKDKLKLFRELEIIIIDEVSMLRADVLDMMDFSLRFTRRSTKPFGGVQMLFIGDLYQLPPVVRDENILMQYYDSSFFFSSLALQQLPLITVELTTVYRQTDEIFVNLLNAIRDREREKIDFNLLNERYDPDFEPTKESFVYLTSHNRMADEVNRKKLSELGGKSYFYGARVVGDFKETQYPNDVEIELRVGAQVMFIRNDTSGDRRYYNGKLAQVTRLAEDEVWVRLEDSDEEFKLRTESWEQKAYSLDTEKNIVEDVLGSFEQYPIRLAWAVTIHKSQGLTFDRVIVDAGKSFTSGQVYVALSRCRTLEGIVLKSKITPEIIFANYQVDNFQYATNANERIEEILESEKYDYAINKMLMSIDSHWLQEQLERWYSVAITSKNLDKDKAKTLYHIINQENKNLIQIYTKFEKIVLQKLQKFIYGEILWQEIESKAKGAVNFFFTTIYSKIFEELKQFYAETKGVKGLKLYNEEIRILIDDLEDYLNDLKQIRLLEMKLFEEKNEVKVSKKIAKIPTHIITYQLFEAEKSIPEIVKERGLAISTIYGHLAKFAEQGVLDIGRIVTQEKLLLFEQEFHKPTHPTTLTDWKKILPPEFEFHEIRLLINHFSYSTAHLSK
>NZ_CP029149.1|WP_120489022.1|1904290_1904872_-|DUF479-domain-containing-protein
MNYLAHSYLNETEEQLVGQFLNDYIRNRDRHLLPEGIQDGIRRHRAIDSFTDTHPAIIEAKKVFAPLTRLYAGAFVDVAMDYFLANDPKILSTTEWKAHSQATYATLRNYLYLFPENFKTVLHYMEKDDWLYNYRTDWGMKHSLQNVLNKAKYLDKSLPIFDAFLKEKPFLQSCYDAFFPELRATVVVLDFKP
>NZ_CP029149.1|WP_120489021.1|1904948_1906292_-|DNA-repair-protein-RadA
MAKLKTSYFCQNCGMQYSKWLGQCQNCGEWNTIVEEVVEKKSKSILPKTKQHIINIIEVETSEEPRIKTPSEELNRVLGGGIVLGSVTLIGGEPGIGKSTLLLQLALKMKKRILYVSGEESASQIKMRADRLTELQNPNCYLFTETSIEKIIYEAKKLQPDFMIIDSIQTLHSAEIESSAGSVSQIRECSNEIIKYAKENNTPVFLVGHITKDGQIAGPKVLEHMVDVVLNFDGDRNHLFRLLRANKNRFGSTSEIGIYEMISQGLKEIKNPSQILITKKLEELSGNAIAVTLEGNRPMLLEIQALVSTAVYGTPQRSSTGFDAKRLNMLLAVLEKRAGFQLGAKDVFLNITGGIKTDDPALDLAVIASILSSNEDIAISERYCFAGEIGLSGEIRPVSQIEQRISEAEKLGYEKIFVSSLNKISKKKYGIKIEEVGKIEDFVELLF
>NZ_CP029149.1|WP_160224611.1|1906376_1908191_+|TonB-dependent-receptor
MKKTFLTVLILAATVSFAQEDTKEVEEVLIQGKFLSTPYQKIVENIEVISKKEIENSPAQSIDELLQQFSGLDIRKRGANGVQSDISLRGGTFDQVLILVNGIPMNDAQTGHNVMNLPIDLSAIEKIEILKGPAARRFGNNAYAGAINIITKPSAEEKVKIKAEGGDFQTYALGLVSSFGTDKFQNLLQTTSTGSQGYKHNTDYTVRNVFYQGKIPLNNGSFGVQAGFSEKKFGANGFYASRKATEQYEEVQTSLVSFNYAQKFQHFALNSSVYWRRGQDMYLYNRQKPEIYRNMHITHNIGGTLNASYQWLLGTTGLGTEVRNEGIVSNNLGERDRFITQVFFEHNFSFFNDNLKITPGVTWAKYSSVGDYFYPGVDIGFRFNPHHKIYGNIAKVHRVPTFTDLYYKSKTEEGNPDLKSESALSAEVGYAFQMKNFSFKVSGFGRDTDNMIDWNFETLDNKWHSQNLVATRVTGFEASSELSLPFINTTFGLSYTYLNNELKSDKVSDKSKYILENLRHQLVAKMENRVLGNFYNQTIYRYQDRQMGGYSINTLDEKLSYRKNGFETYVVINNLTNNKYTDAFGIEMPGRWFHIGVSYTIGIN
>NZ_CP029149.1|WP_120489020.1|1908317_1909790_-|amidophosphoribosyltransferase
MKDLEVFKKEYLQRIKKQSYGRNTFRTKDEERLDAPNEECGIFGLYSENEVDTFSLSQFGLFALQHRGQEACGISVSKNGHIVNIKDEGLVLDVFKGINEPETFMGNSVIGHTRYTTAGDKKKYNYQPFFAKNEWDQIILSIAHNGNLTNAKQLRTELEAEGVVFKATSDSEIILRLIQKNLDLGLRGAIKHTMERIEGAFSVVGMTRNKFFAFRDFNGIRPLVLGALDEKTFVVASESAALDAVGAAYVRDILPGEIIYTSSDEKGLKSYLVKDDCVNRICAFEYIYFARPDTTLENINVYEVREKSGMKIWEQSPVEADIVIGVPDSGVPAAIGFSKASGIPFSPVLVKNRYIGRSFIVPTQEMRERIVNLKLNPIVSEIKGKRIVIIDDSIVRGTTSKRLVKILKDAGVKEIHFRSVSPPIIAPCFLGIDTPSKDDLISANMSVEELRDYLGVDSLDFLSLENLKDILGSSDHCFGCFTEIYPVKSP
>NZ_CP029149.1|WP_160224612.1|1909805_1910525_-|phosphoribosylaminoimidazolesuccinocarboxamide-synthase
MNQKLEMLYEGKAKQIYATENPEEIIVYFKDDATAFNAQKKGQVKLKGEMNNAITTLIFEYLQTKGIPTHFIKQLNEKEQLVKKVTIIPLEFVVRNYAAGSMAQRLGVEEGIKSPVTIFDICYKDDALGDPLINDHHAVFLGAASYEELGEMYALAGKINDALKELFDKINIILVDFKIELGKTADGKIILADEISPDTCRLWDKDTLKKLDKDRFRRDLGDVTEAYVEIYHRLKALLG
>NZ_CP029149.1|WP_120489018.1|1911077_1912451_+|signal-recognition-particle-protein
MFNSLQDKLDKALHSLSGRGKITEINVAETVKEIRRALVDADVNYKVAKDLTKRVQDKAIGQNVLTSLTPGQLMTKIVHDELVELMGGSQEGINLSGKPSIILIAGLQGSGKTTFSGKLSNFLKTKKSKKPLLVACDVYRPAAIDQLKVLGTQTGVEVYTEEGNKNPALIAENAIHYAKSNGFDVVIIDTAGRLAVDEEMMNEIKTVHQTIKPQETLFVVDSMTGQDAVNTAKAFNDVLNFDGVVLTKLDGDTRGGAALTIRSVVEKPIKFISTGEKMEALDLFYPERMADRILGMGDVVSLVERAQEQFDEEEAKKLQKKIAKNEFGFDDFLKQINQIKKMGNMKDLVGMIPGVGKAVKDIDINDDAFKHIEAIIYSMTPEERRKPSIINTQRKNRIAKGSGRKLEEVNQLMKQFDQMGKVMKMMQGPQGKQMMQMMSKMGGNMPGLGGLGKMFGR
>NZ_CP029149.1|WP_160224613.1|1912465_1914604_+|OmpA-family-protein
MKRKVIVAGVLLGIFSTTELSAQKYLGLSNSNYSGVYGGQYSPAKVADKKVRLSVNLISVNAMLDNDYYKFTGVDNFKDLGLSTLGQGLSYDAGQKRLSFGVIGETLAPSFQFTTGDRLGFGFSSRIRTFAQGDNINSDFINVLNKNFKNNIAIKDNQEFSLNANGILDLGVKGAYTVVDNDKLRLSLGAALKYYRGLAYNSFISKRYDLNYNFSITNSTINFNNIDWEFYTNLDNENLEETLRKPFSSPNAGTGFGGDFGAELELKGNNAEKPYAFKFGIAVNDIGSIKYKNLNFMSIKGSGVNIDASSIDLLDLNSTADYLQSKGLSVVRSTNRELTTSLPTNLNVYGDYAITKKFFISANASINVVKTNSTNPYYYNFVGVAPRFESKWFDVSVPLSYNLMSKDFKPGLAFRVGPLSLGSDDLKLLFTESKGANAYLGLHFELFKKQAKAIVPPVESPIDSDGDGVFDKDDQCPYIAGPVENNGCPWPDTDGDGVLDKDDACPDVAGAIENNGCPWPDTDGDGVLDKDDKCPTVPGLVENFGCPKAHETVAKEVTLALKDILFNFGKATINPESNKKLDTAAKIIKDSKGGTYLLVGHTDKKGNEAYNLKLSRERAAAVVQALEERGVPADQLKSKGVGSKEATTPATASDAERQKDRRVEVLHITGSEWEALSKSDVPVAKKKVATSAKGKAPAKKAPVRKVAPKKKK

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Crispr_ID: NZ_CP029149_12

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP029149_12

1973874-1973972

Orphan

Consensus_repeat	Method
GGCATTCAACCAAGACCTCTCCAA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP029149_12

>merge|NZ_CP029149|12|1973874-1973972|CRISPRCasFinder
GGCATTCAACCAAGACCTCTCCAAATGGAATGTGAGCAAAGTAGAAAATATGAGCTATATGTTTAATGGCGCTACGGCATTCAACCAGGACCTCTCCAA

>NZ_CP029149|12|11|1973874-1973972|CRISPRCasFinder
GGCATTCAACCAAGACCTCTCCAA	ATGGAATGTGAGCAAAGTAGAAAATATGAGCTATATGTTTAATGGCGCTAC
GGCATTCAACCAGGACCTCTCCAA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP029149.1\|WP_160224637.1\|1970127_1971378_+\|BspA-family-leucine-rich-repeat-surface-protein	unknown	unknown	gnl\|CDD\|308794
NZ_CP029149.1\|WP_120488973.1\|1963513_1964818_+\|30S-ribosomal-protein-S12-methylthiotransferase-RimO	unknown	unknown	gnl\|CDD\|273453
NZ_CP029149.1\|WP_160224634.1\|1964948_1965692_+\|electron-transfer-flavoprotein-subunit-beta/FixA-family-protein	unknown	unknown	gnl\|CDD\|238847
NZ_CP029149.1\|WP_120488956.1\|1983686_1984577_-\|endonuclease	unknown	unknown	gnl\|CDD\|197317
NZ_CP029149.1\|WP_160224635.1\|1967324_1967921_-\|WbqC-family-protein	unknown	unknown	gnl\|CDD\|378083
NZ_CP029149.1\|WP_160224636.1\|1967920_1969597_-\|signal-peptidase-I	unknown	unknown	gnl\|CDD\|182787
NZ_CP029149.1\|WP_120488965.1\|1975554_1976256_-\|4-hydroxy-tetrahydrodipicolinate-reductase	unknown	unknown	gnl\|CDD\|234595
NZ_CP029149.1\|WP_120488972.1\|1965716_1966667_+\|electron-transfer-flavoprotein-subunit-alpha/FixB-family-protein	unknown	unknown	gnl\|CDD\|224936
NZ_CP029149.1\|WP_160224643.1\|1979875_1980688_-\|purine-nucleoside-phosphorylase	unknown	unknown	gnl\|CDD\|350160
NZ_CP029149.1\|WP_160224642.1\|1978736_1979570_-\|energy-transducer-TonB	unknown	unknown	gnl\|CDD\|367555
NZ_CP029149.1\|WP_160224632.1\|1960897_1962412_+\|bifunctional-phosphoribosylaminoimidazolecarboxamide-formyltransferase/IMP-cyclohydrolase	unknown	unknown	gnl\|CDD\|234854
NZ_CP029149.1\|WP_160224645.1\|1981742_1982798_-\|3-dehydroquinate-synthase	unknown	unknown	gnl\|CDD\|341474
NZ_CP029149.1\|WP_160224640.1\|1976879_1977770_-\|ParB/RepB/Spo0J-family-partition-protein	unknown	unknown	gnl\|CDD\|275105
NZ_CP029149.1\|WP_160224633.1\|1962684_1963350_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_160224638.1\|1971438_1973121_+\|BspA-family-leucine-rich-repeat-surface-protein	unknown	unknown	gnl\|CDD\|308794
NZ_CP029149.1\|WP_160224644.1\|1980671_1981712_-\|tetraacyldisaccharide-4'-kinase	unknown	unknown	gnl\|CDD\|376853
NZ_CP029149.1\|WP_120488964.1\|1976273_1976864_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_120488971.1\|1966741_1967299_-\|RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|224511
NZ_CP029149.1\|WP_160224641.1\|1977807_1978569_-\|ParA-family-protein	unknown	unknown	gnl\|CDD\|379293
NZ_CP029149.1\|WP_120488957.1\|1982912_1983659_-\|deoxyribose-phosphate-aldolase	unknown	unknown	gnl\|CDD\|188646

Protein	Function_ID	Function_description	E-value
NZ_CP029149.1\|WP_160224637.1\|1970127_1971378_+\|BspA-family-leucine-rich-repeat-surface-protein	gnl\|CDD\|308794	pfam03382, DUF285, Mycoplasma protein of unknown function, DUF285. This region appears distantly related to leucine rich repeats.	1.19154e-49
NZ_CP029149.1\|WP_120488973.1\|1963513_1964818_+\|30S-ribosomal-protein-S12-methylthiotransferase-RimO	gnl\|CDD\|273453	TIGR01125, Ribosomal_protein_S12_methylthiotransferase_RimO, ribosomal protein S12 methylthiotransferase RimO. Members of this protein are the methylthiotransferase RimO, which modifies a conserved Asp residue in ribosomal protein S12. This clade of radical SAM family proteins is closely related to the tRNA modification bifunctional enzyme MiaB (see TIGR01574), and it catalyzes the same two types of reactions: a radical-mechanism sulfur insertion, and a methylation of the inserted sulfur. This clade spans alpha and gamma proteobacteria, cyano bacteria, Deinococcus, Porphyromonas, Aquifex, Helicobacter, Campylobacter, Thermotoga, Chlamydia, Streptococcus coelicolor and Clostridium, but does not include most other gram positive bacteria, archaea or eukaryotes. [Protein synthesis, Ribosomal proteins: synthesis and modification].	4.63105e-163
NZ_CP029149.1\|WP_160224634.1\|1964948_1965692_+\|electron-transfer-flavoprotein-subunit-beta/FixA-family-protein	gnl\|CDD\|238847	cd01714, ETF_beta, The electron transfer flavoprotein (ETF) serves as a specific electron acceptor for various mitochondrial dehydrogenases. ETF transfers electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase. ETF is an heterodimer that consists of an alpha and a beta subunit which binds one molecule of FAD per dimer . A similar system also exists in some bacteria. The homologous pair of proteins (FixA/FixB) are essential for nitrogen fixation. The beta subunit protein is distantly related to and forms a heterodimer with the alpha subunit.	4.8673e-57
NZ_CP029149.1\|WP_120488956.1\|1983686_1984577_-\|endonuclease	gnl\|CDD\|197317	cd09083, EEP-1, Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1. This family of uncharacterized proteins belongs to a superfamily that includes the catalytic domain (exonuclease/endonuclease/phosphatase, EEP, domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds. Their substrates range from nucleic acids to phospholipids and perhaps, proteins.	4.17024e-12
NZ_CP029149.1\|WP_160224635.1\|1967324_1967921_-\|WbqC-family-protein	gnl\|CDD\|378083	pfam08889, WbqC, WbqC-like protein family. This family of proteins are functionally uncharacterized. However it is found in an O-antigen gene cluster in E. coli and other bacteria suggesting a role in O-antigen production. Feng et al. suggest that wbnG may code for a glycine transferase.	3.51567e-30
NZ_CP029149.1\|WP_160224636.1\|1967920_1969597_-\|signal-peptidase-I	gnl\|CDD\|182787	PRK10861, PRK10861, signal peptidase I.	1.46346e-15
NZ_CP029149.1\|WP_120488965.1\|1975554_1976256_-\|4-hydroxy-tetrahydrodipicolinate-reductase	gnl\|CDD\|234595	PRK00048, PRK00048, dihydrodipicolinate reductase; Provisional.	6.26125e-59
NZ_CP029149.1\|WP_120488972.1\|1965716_1966667_+\|electron-transfer-flavoprotein-subunit-alpha/FixB-family-protein	gnl\|CDD\|224936	COG2025, FixB, Electron transfer flavoprotein, alpha subunit [Energy production and conversion].	3.1364e-94
NZ_CP029149.1\|WP_160224643.1\|1979875_1980688_-\|purine-nucleoside-phosphorylase	gnl\|CDD\|350160	cd09009, PNP-EcPNPII_like, purine nucleoside phosphorylases similar to human PNP and Escherichia coli PNP-II (XapA). Human PNP catalyzes the reversible phosphorolysis of the purine nucleosides and deoxynucleosides inosine, guanosine, deoxyinosine, and deoxyguanosine. Patients with PNP deficiency typically present with severe immunodeficiency, neurological dysfunction, and autoimmunity. Escherichia coli PNPII, product of the xapA/pndA gene, catalyzes the phosphorolysis of xanthosine, inosine and guanosine with equal efficiency and has been referred to as xanthosine phosphorylase and inosine-guanosine phosphorylase. E. coli PNPII is also capable of converting nicotinamide to nicotinamide riboside, and may be involved in the NAD+ salvage pathway. It is one of two purine nucleoside phosphorylases found in E. coli, which also contains PNPI, which displays a different substrate specificity and belongs to a different subgroup of the nucleoside phosphorylase-I (NP-I) family than PNPII. NP-I family members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.	6.90996e-151
NZ_CP029149.1\|WP_160224642.1\|1978736_1979570_-\|energy-transducer-TonB	gnl\|CDD\|367555	pfam03544, TonB_C, Gram-negative bacterial TonB protein C-terminal. The TonB_C domain is the well-characterized C-terminal region of the TonB receptor molecule. This protein is bound to an inner membrane-bound protein ExbB via a globular domain and has a flexible middle region that is likely to help in positioning the C-terminal domain into the iron-transporter barrel in the outer membrane. TonB_C interacts with the N-terminal TonB box of the outer membrane transporter that binds the Fe3+-siderophore complex. The barrel of the transporter, consisting of 22 beta-sheets and an inside plug, binds the iron complex in the barrel entrance.	1.25793e-05
NZ_CP029149.1\|WP_160224632.1\|1960897_1962412_+\|bifunctional-phosphoribosylaminoimidazolecarboxamide-formyltransferase/IMP-cyclohydrolase	gnl\|CDD\|234854	PRK00881, purH, bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional.	0
NZ_CP029149.1\|WP_160224645.1\|1981742_1982798_-\|3-dehydroquinate-synthase	gnl\|CDD\|341474	cd08195, DHQS, Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway, which involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds, is found in bacteria, microbial eukaryotes, and plants, but not in mammals. Therefore, enzymes of this pathway are attractive targets for the development of non-toxic antimicrobial compounds, herbicides and anti-parasitic agents. The activity of DHQS requires nicotinamide adenine dinucleotide (NAD) as cofactor. A single active site in DHQS catalyzes five sequential reactions involving alcohol oxidation, phosphate elimination, carbonyl reduction, ring opening, and intramolecular aldol condensation. The binding of substrates and ligands induces domain conformational changes. In some fungi and protozoa, this domain is fused with the other four domains in shikimate pathway and forms a penta-domain AROM protein, which catalyzes steps 2-6 in the shikimate pathway.	1.98262e-144
NZ_CP029149.1\|WP_160224640.1\|1976879_1977770_-\|ParB/RepB/Spo0J-family-partition-protein	gnl\|CDD\|275105	TIGR04285, parB-like_partition_protein, nucleoid occlusion protein. This model describes nucleoid occlusion protein, a close homolog to ParB chromosome partitioning proteins including Spo0J in Bacillus subtilis. Its gene often is located near the gene for the Spo0J ortholog. This protein bind a specific DNA sequence and blocks cytokinesis from happening until chromosome segregation is complete.	2.82268e-85
NZ_CP029149.1\|WP_160224638.1\|1971438_1973121_+\|BspA-family-leucine-rich-repeat-surface-protein	gnl\|CDD\|308794	pfam03382, DUF285, Mycoplasma protein of unknown function, DUF285. This region appears distantly related to leucine rich repeats.	6.52878e-50
NZ_CP029149.1\|WP_160224644.1\|1980671_1981712_-\|tetraacyldisaccharide-4'-kinase	gnl\|CDD\|376853	pfam02606, LpxK, Tetraacyldisaccharide-1-P 4'-kinase. This family consists of tetraacyldisaccharide-1-P 4'-kinase also known as Lipid-A 4'-kinase or Lipid A biosynthesis protein LpxK, EC:2.7.1.130. This enzyme catalyzes the reaction: ATP + 2,3-bis(3-hydroxytetradecanoyl)-D -glucosaminyl-(beta-D-1,6)-2,3-bis(3-hydroxytetradecanoyl)-D-glu cosam inyl beta-phosphate <=> ADP + 2,3,2',3'-tetrakis(3-hydroxytetradecanoyl)-D- glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate. This enzyme is involved in the synthesis of lipid A portion of the bacterial lipopolysaccharide layer (LPS). The family contains a P-loop motif at the N-terminus.	1.42215e-87
NZ_CP029149.1\|WP_120488971.1\|1966741_1967299_-\|RNA-polymerase-sigma-factor	gnl\|CDD\|224511	COG1595, RpoE, DNA-directed RNA polymerase specialized sigma subunit, sigma24 homolog [Transcription].	1.8972e-29
NZ_CP029149.1\|WP_160224641.1\|1977807_1978569_-\|ParA-family-protein	gnl\|CDD\|379293	pfam13614, AAA_31, AAA domain. This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop.	1.97107e-92
NZ_CP029149.1\|WP_120488957.1\|1982912_1983659_-\|deoxyribose-phosphate-aldolase	gnl\|CDD\|188646	cd00959, DeoC, 2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family. 2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family. DERA belongs to the class I aldolases and catalyzes a reversible aldol reaction between acetaldehyde and glyceraldehyde 3-phosphate to generate 2-deoxyribose 5-phosphate. DERA is unique in catalyzing the aldol reaction between two aldehydes, and its broad substrate specificity confers considerable utility as a biocatalyst, offering an environmentally benign alternative to chiral transition metal catalysis of the asymmetric aldol reaction.	3.30991e-53

>NZ_CP029149.1|WP_160224638.1|1971438_1973121_+|BspA-family-leucine-rich-repeat-surface-protein
MKKISILFALFVAIVAYAQEPFVGVWNAPRGQIVFATEGEFSYSYEKVGNPSIKGIGDGWPNRTELFVSPGKYKISIVPKNNNKFRFKDLNNFLEVQKWGSVKWADDLSGMFANCNELQITADDTPDLSGVTSLSGLFSGCSSLETINGLNDWDVSNVQDMSYMFSGATHFNQDLFRWNMGNVKNVSYMFQEASTFNGDIHTWEFKNLENMEYMFREAFAFNGDVSNWNVGTVTNMKGVFYRAKAFSGDVSNWNVSQAKNMEVMFYEALQFNSDLSRWDVGNVTLMYAMFSKAPLFNSDLSNWNVSNVTGTWSMFQGATAFNSDISRWDVSKVTDMNNMFKEAEAFNQDISQWDVSKVTNMGSMFESTKNFNKDISNWDVSSVQVLDFMFEDAKAFNQSLAGWKIKDKAHMTNFLKESGMDCENYSKTLKGWADNPNTGKEIHFYSTASYGDSAKPYRQKLIDEKDWKIYSDSYDSSCTADLATETVAQRPQFFIIKPVKEELHIQGLDGIKSIEIYSANGSLVKTLNANQRGVSNLSKGVYILKINTQNGTYTDKIIKD
>NZ_CP029149.1|WP_160224637.1|1970127_1971378_+|BspA-family-leucine-rich-repeat-surface-protein
MKKISILFALCLAIVAYAQGNPLIGVWKSDASGVVELSASGDFSYTYEKVGEPSVSGSGSAVAVGTEFQLKITESVGEYTIKINPTGVFRLKKNGGDAFRNLSQWGDIDWAEDLSGMFRECSQLKITATDTPDFSKVTDMSRMFLNCEQLENVPNINEWAVGEVTDMESMFEGAKQFNGDISQWKVGKVETMVSMFKGAEAFNQDLSQWDTEALTETVSMFRGAKAFNKDISGWKVQNISLMSSMFYDATNFSQDLGAWKIKTGATLAGIFRNSGMDCESYSKTLKGWAENSEVGTSVNLSTNSKYGDAAKPYRDELIKKKGWTISSDKYDDKCTVDLGIADTPTRPALKVLKPVKDELIISSPEEIKNIEIYTASGALIKTLKGKQRAVSNLPKGLYILKINTENHQYTEKIIKE
>NZ_CP029149.1|WP_160224636.1|1967920_1969597_-|signal-peptidase-I
MEYFVQYTVFVLILSALMGLSTWKLFRKMGHHPLLAFVPFYNYFLILKVSKKPKWWALLAYMPIVGSIMMTVFHLLLMEKFGKKLFPQKFLTVVLPFIYMAYINYFDDAEIDEMEDLFLTEEERQEKKKDTLIGSLTFAAVFATIIHTFVTQPFGIPTGSMERTLLVGDFLFVNKWSYGFRMPTRPLAIPFLQSTIMDTGEKGNPKDDPKSYVDAVELPYLRIFSSEPQRNDIVVFNYPDDSVHTAIDRKDPYVKRLLATAGDVLEIKAGKVFINGKPEKRMADAEVQHSYTVTTEQLLDIDAIFKAYGVLPFEEKDGVYVFSGLTDAMVKDFKAMPGVTSVEENIDPKGEKTVGYYINKVKSMEEGELVLSNKINYSNTIFPHNKNWNPDWYGPLRIPKKGDVISLTEDNLPEYQKLITQYEGNTLVHKDGKFFINGKETDQYTVKYNYYMMIGDNRDNSLDARFFGFVPETHIMGKPMFAWLSLQGLFSDSERGVSYSEGKIYQAPFKIRWERMFKAVNTGDANKTSYWWLAVLILTLFFGWDYIMKIFKKKKEDE
>NZ_CP029149.1|WP_160224635.1|1967324_1967921_-|WbqC-family-protein
MNLLPVFYLPPVSWFARFIAQEDITLEQYENFPKQTYRNRANIYSANGKLSLIIPIKHTGDRLMKDIQISYAENWQKLHWKSIKTAYQSSPYFEYYEDKLQSIFETREPSLLKFNLRALEVLQRILKTDKGFLLTEEYIKQPQMNDYREKFSAKKKPHYGFEEYYQTFSDKMGFIEDLSVLDLICNKGPEALAYLQNI
>NZ_CP029149.1|WP_120488971.1|1966741_1967299_-|RNA-polymerase-sigma-factor
MEQKQILQLIQLAREKDQKSQTALINLYWVEVFSFVMKKVQHENLADEITVNVFSKVLSKLHLYDSDFQFKTWVLTIAQNTIIDYWRKKAREAEDTDGNLEEVKNEFAKSPEELLISEEEHKKIQDIVSTMDANYAEIIRLRFFEEMSIKEIAEVLNISIANTKVRIMRAKKVLAQLLKENDFSH
>NZ_CP029149.1|WP_120488972.1|1965716_1966667_+|electron-transfer-flavoprotein-subunit-alpha/FixB-family-protein
MTIFVYAENNNGSYKKTTFEAISFAKAIAESNGGNVTAITINPTDSVEKLYQYGADKVLTIKNEGLKFSPKAYSQILAEVAQSELIILPNTVDSSSIAPMLAVQKGFSIITNVTELPESLSPLRVKRKVFSGKAFATVQSETTGTVLTLATNSFGVKENPQSSAGTEEIINSTVQNTDVQVISTEQSIGKLDLKDADIVVSGGRGLKDAEHWHLIEELASALGGATACSKPVSDMGWRPHSEHVGQTGKTISPNLYIAAGISGAIQHLAGVNSSKTIVVINSDSEAPFFKAADYGVVGDVFQVLPELTKKIKEANT
>NZ_CP029149.1|WP_160224634.1|1964948_1965692_+|electron-transfer-flavoprotein-subunit-beta/FixA-family-protein
MNILVCISSVPDTTSKINFTADSSALDKSGIQWIINPVDEVCLSKAVKLQSSGAKVSVLCIGEGETEAVLRKCLAIGADEAIRVNLSPKDSYSTAKEIEQVVKSGNYDVILCGKESMDYNNGAVAGILAALLGYPFVNSAIEIELQANEAKITREIDGGTETVAVQLPAVIGGQKGLVSEKDIIIPNMRGIMSARTKPLQVLEPTSNEVKANTLSFENTPARANVKLIEANNLDELVRLLKEEAKVI
>NZ_CP029149.1|WP_120488973.1|1963513_1964818_+|30S-ribosomal-protein-S12-methylthiotransferase-RimO
MRTKSVGRKKINIVTLGCSKNLYDSEVLMGQLKASGKEVSHEAKNGDIIVINTCGFVDVAKEESVNTILDYIEAKKRGDVEKVFVMGCLSERYKPDLQKEIPDVDEYFGTKDLPILLKHLGADYKHELVGERMTTTPKHYAYLKISEGCDRPCSFCAIPLMRGNHISVPIEKLVLEAKKLAQKGTKELILIAQDLTYYGLDIYNKRALADLLKELVKVEGIEWIRLHYAFPTGFPEDVLEIIKNEPKVCNYIDIPLQHINTEILKSMKRGTTREKTNTLLNKFREKVPDMAVRTTLIVGYPGETEEAFQELKEWVKEQRFDRLGCFTYSHEENTTAFDLQDDVPQEVKEARVSEIMELQSSISWEKNQEKVGKVFRCIFDRKEGNYFVGRTEYDSPDVDNTVLVSAENLYLPIGEFADIRITSAEEFDLYGELA
>NZ_CP029149.1|WP_160224633.1|1962684_1963350_+|hypothetical-protein
MKISVLSHISTVNLAAFTELVIKISKSEKYKIDTENHYLKDIENEYNIYKKSHTKQTHNGKEKELTKTDRERDYLFNGIKSFLKGCIKLPIHPFSEEAKSLYEVFKFHDLYLNRLPYEDKSTLLRELLEALELKINKERIKILLLETSIGKLKDTQERFDILYSEQVEANTNLREIQSASAIRKSLEKALRDYLIYVNSAQLLPNWKELQLELKELLKTIK
>NZ_CP029149.1|WP_160224632.1|1960897_1962412_+|bifunctional-phosphoribosylaminoimidazolecarboxamide-formyltransferase/IMP-cyclohydrolase
MKKRVLISVSDKSGLAEFALFLEKNKYEIISTGGTFKYLKESGAHPIPIDDVTQFPEMLGGRVKTLHPKVHGGLLALRDNPEHIQTVAEHGIELIDMVIVNLYPFFENATKNIDLEEKVEFIDIGGPSMLRSAAKNFKSVTVITDVADYQKVQQEIETTGNSTLETRKYLAGKVFNLTSAYDAAISKMLLSCEYPDYLNASYKKVADLRYGENPHQSAAYYVSTVEQGAMKDFEQLGGKELSFNNLRDMDLCWKVVSEFKEQLACCAVKHSTPCGVSIGSTPLETYSKTFECDPISIFGGIVAMNFTVDAPTAEELNKTFLEIVMAPDFSTEALDILRKKKNLRIIKIKNPVSDKQTWVKIDGGLLVQDCDHHFSNEIQVVTEQKPSPELRDALLFAQRVVKYVKSNAIVVSNGTQALGIGGGQVNRIWATQQAIERAKEKFSGDLVLASDAFFPFRDVVDFCAEHHIKAIIQPGGSMRDSESIQAANEHGIPMLFTGIRHFLH
>NZ_CP029149.1|WP_120488965.1|1975554_1976256_-|4-hydroxy-tetrahydrodipicolinate-reductase
MKIALVGYGKMGQIIDRIATERGHEIVARLNQTPTSETLNNADVAIEFSQPEVAFQNIKTCLENHTPVVCGTTGWLSRKPEIEQIAQAQQSAFLYGSNFSLGVNLFFALNEKLALMMAHFDEYNAQLEEIHHIHKKDAPSGTAISLAEGLIAHHPKFHLWKLDETEGAQLGIFAIREDEVPGTHSVFYRSKVDEIEIKHTAFSREGFALGAVVAAEWLRDKKGIFSMKDVLGV
>NZ_CP029149.1|WP_120488964.1|1976273_1976864_-|hypothetical-protein
MKKLLLIISCFIIHLAFSQEVDTLKVAPQTVQDIERDIQMINKPLKITPNSPVKAGLYSAVLPGLGQYYNKKYWKIPIVWGGIGTGVGIVLWNQRKYDKYRSAFIAELNGQPHEFSGFQGVNEEVLGRIQDKFKRQRDYAIAITGLIYVLNIIDAVVDAHLYEMKRDPNLTLKPTVIYDEYAEQNAKAGISLSFRF
>NZ_CP029149.1|WP_160224640.1|1976879_1977770_-|ParB/RepB/Spo0J-family-partition-protein
MKDKKRAMGRGLGAILNSESKNTIHTATDAGAEKLVGNIVEVPIEDIYPNATQPRTYFDEKALTDLAQSIKSLGVIQPITLRKDKDKFEIISGERRFRASKLAGLKTIPAYIRLVNDQELLEMALVENIQREDLDAIEVALTYQRLLEEIGLTQENLSQRVGKERSTITNSLRLLRLTPEIQNAIRSAAISAGHGRAILSLDTEEEQQQLFEQIIKEELNVRQAEALASAIKNPKEKKTKAQREISNYHKKVQKNLSDLLDTKVEIKTSANGKKGKLVLDFKNEAVLEEILAYFNR
>NZ_CP029149.1|WP_160224641.1|1977807_1978569_-|ParA-family-protein
MAKIIGIANQKGGVGKTTTAVNLAAALGVLEKKVLIIDADPQANATSGLGVEEVRNSTYNLLEHSENVEDCIYKTSSPNLDIIPSHIDLVAAEIELVDKENREYMLRTALEPIKNQYDFIIIDCAPSLGLITINALTAADSVIVPIQCEYFALEGLGKLLNTIKNVQNIHNPDLSIEGLLLTMYDSRLRLSNQVVEEVNMHFPEMVFETVISRNVRLSEAPSFGESILMYDAESKGAVQYIQLAEEVLLKNKK
>NZ_CP029149.1|WP_160224642.1|1978736_1979570_-|energy-transducer-TonB
MKNLFKKEEFLLDEVIFQGRNKEYGAYDLRYQSDKMLTKAMFIGVAFFGSVSIIPLVTSLFKEEPKATVEVVARPMDIENIEKKEDEKPLPEKSITPPKPQKVNTVDSRVPDPKRNATNESSVPTNEESLNAIRGLETIQGKSPDIRLNPSSNETNNSGNTGEVKFEKPVIIDDSPKTKVDVSADFIGGIDAFRNKVMSSFDISEFEESNEKLSTEITFVVEKDGSISNIKASGKDDAFNKETIRAIKSIKGKWTPAKIDGQPVRSYFRFPVSVVFN
>NZ_CP029149.1|WP_160224643.1|1979875_1980688_-|purine-nucleoside-phosphorylase
MLNKIKETAEFIKGIIKETPDFAIVLGSGLGALKNEVEPIHTLEYSEIPNFPQTTVVGHGGKLIYGNLEGKKVLMMSGRFHYYEGHDIKTVVFPFRVFHALGIKNLIVSNASGGVNKDFRVADVMIIRDHINMMPEHPLRGKNIDEFGPRFVDMSEPYSRKMIEIAEKVATEKGIKVHQGVYVALQGPTFETPAEYGLVKAIGGDAVGMSTVPEVIVAKHQGMDCFGISIITDLGGPDIAFTVSHDEVLQAAEKAMPNVISIVKGVVKNY
>NZ_CP029149.1|WP_160224644.1|1980671_1981712_-|tetraacyldisaccharide-4'-kinase
MKRWYLYPFSLVYHLATATRNLAYSIGILKSTRFRTPIINVGNLSVGGSGKSPMVMYLADLLSQYYRTGVLSRGYGRQTKGYRITNYDSNYRQVGDEAMQLFERFKNRFVIGVCEDRVEGAKKMIPDMDLKVLLLDDAYQHRAIKAGFNILMTDYNDPYFKDFLLPAGNLRESRVGAKRAQVIMVSKCPDNLTEEKKQYYISRIKPTQNQKVFFSSISYDEKVFGKDGLGKPTELPDNNLAYYDILLITGIANPKPLLEHLSKFNKNFKHLKFKDHHNFTDADIKKIMDEYRKLGDYKLILTTEKDYVRLKTFDYLRGLIFYWPINLSIDKKEEFNQIIIDYVKQN
>NZ_CP029149.1|WP_160224645.1|1981742_1982798_-|3-dehydroquinate-synthase
MISILDTQFSLLNLYLSEALPTKIFILCDENTNEYCLPTLLLNMQTDIPFEIIEIEAGEEMKTIETATQLWEILADFGADRKSLLINLGGGVITDLGGFVASTYKRGIRFVNMPTSLLAMCDASIGGKTGIDHQFLKNVVGTFAHPEAVFVYPNFLDSLPFVELRSGFAEMLKHGLIASRSHWENLSSLSEINVAAVSPYIKESMMIKEKVVSIDFKEENIRKTLNFGHTIGHAIESLFLEQGSLVPHGEAVAAGMICETYLSCLEGLINRETRDNIINTIRKFYPVLNIQNFTDEALISLMANDKKNTSGKINFSLISAVGSGIYDYQSTEKNIIESIEFYGSLPKDSFY
>NZ_CP029149.1|WP_120488957.1|1982912_1983659_-|deoxyribose-phosphate-aldolase
MNVENFLDSTYLKLPEQSGLTTEETRKKVIELTDEAINYHFFEVMIRPEYVHFIKNYIKEKSASVKVGTVIGFHEGTASVEAKLAEAEKAIADGVDELDFVINFEKFKANELAYVKDEFLKCTALALKHHKTAKWIIEIAALTDEQIASITSHIRQWAEESFAGREQEIFVKSSTGFYKTEGGKPNGATPEAIKIMIAHAGKLPVKAAGGVRTHQEALDMIALGVKRIGTSSALALSGKGTAPSSAGY
>NZ_CP029149.1|WP_120488956.1|1983686_1984577_-|endonuclease
MLRAKGNTALLMFYNLENLFYPLSSQNIDNQLRNWSLSRYQKKLKSISETLLLIQKTYGSLPIIIGVCEVQGIQPLEDLIQYPPLSSYGIIHYKGRDKRGVDTALLYDSKEIEVLHSEPLPVSETRSIIFTKIQYCNSIFNVYTLHLPSRRGSDEAKNKREIILNTLKEHLINNLNAQKEPVIILGDFNANPNDEAIRNLMNISPRFQLINPFSEVYANRSFSNFHRSKGLLFDQILFSEHLVSENFPLAFVKAEIFAPEQLKQHGKPSRTFAGSRYLGGQSDHFPVIIQTKTIIN

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Crispr_ID: NZ_CP029149_13

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP029149_13

2000476-2000573

Orphan

Consensus_repeat	Method
CTTGCAGGTGGTGCACTTAGCCACTAGCGTG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP029149_13

>merge|NZ_CP029149|13|2000476-2000573|CRISPRCasFinder
CTTGCAGGTGGTGCACTTAGCCACTAGCGTGAAGCTACAGAGTAGAAAGAGTAGATGTGTATATAGACTTGCAGGTGGCGCACTTAGCCACTAGCGTG

>NZ_CP029149|13|12|2000476-2000573|CRISPRCasFinder
CTTGCAGGTGGTGCACTTAGCCACTAGCGTG	AAGCTACAGAGTAGAAAGAGTAGATGTGTATATAGA
CTTGCAGGTGGCGCACTTAGCCACTAGCGTG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP029149.1\|WP_120488948.1\|1991327_1991858_+\|Rieske-(2Fe-2S)-protein	unknown	unknown	gnl\|CDD\|239550
NZ_CP029149.1\|WP_120488937.1\|2007682_2009047_-\|MATE-family-efflux-transporter	unknown	unknown	gnl\|CDD\|240536
NZ_CP029149.1\|WP_120489692.1\|2010055_2011240_-\|sigma-54-dependent-Fis-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225114
NZ_CP029149.1\|WP_120488944.1\|1997233_1998043_-\|type-I-methionyl-aminopeptidase	unknown	unknown	gnl\|CDD\|238519
NZ_CP029149.1\|WP_160224653.1\|2009574_2009985_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|224514
NZ_CP029149.1\|WP_120488949.1\|1990732_1991308_+\|4Fe-4S-dicluster-domain-containing-protein	unknown	unknown	gnl\|CDD\|319891
NZ_CP029149.1\|WP_160224652.1\|2005406_2007257_-\|type-IIA-DNA-topoisomerase-subunit-B	unknown	unknown	gnl\|CDD\|235501
NZ_CP029149.1\|WP_120488945.1\|1994036_1995377_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|238863
NZ_CP029149.1\|WP_160224648.1\|1999769_2000408_-\|rhomboid-family-intramembrane-serine-protease	unknown	unknown	gnl\|CDD\|366759
NZ_CP029149.1\|WP_120489693.1\|1998051_1998483_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|223319
NZ_CP029149.1\|WP_160224649.1\|2000947_2003527_-\|DNA-gyrase/topoisomerase-IV-subunit-A	unknown	unknown	gnl\|CDD\|237192
NZ_CP029149.1\|WP_120488947.1\|1991875_1992175_+\|C4-dicarboxylate-ABC-transporter-permease	unknown	unknown	unknown
NZ_CP029149.1\|WP_160224651.1\|2004822_2005371_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP029149.1\|WP_160224650.1\|2003527_2004817_-\|TIGR00341-family-protein	unknown	unknown	gnl\|CDD\|377221
NZ_CP029149.1\|WP_120488933.1\|2011818_2012196_-\|large-conductance-mechanosensitive-channel-protein-MscL	unknown	unknown	gnl\|CDD\|376605
NZ_CP029149.1\|WP_120488936.1\|2009349_2009532_+\|type-II-toxin-antitoxin-system-HicA-family-toxin	unknown	unknown	gnl\|CDD\|377942
NZ_CP029149.1\|WP_160224647.1\|1998513_1999773_-\|CinA-family-nicotinamide-mononucleotide-deamidase-related-protein	unknown	unknown	gnl\|CDD\|234789
NZ_CP029149.1\|WP_120489694.1\|1995410_1997066_+\|MBOAT-family-protein	unknown	unknown	gnl\|CDD\|224610
NZ_CP029149.1\|WP_120488934.1\|2011350_2011758_-\|tRNA-(adenosine(37)-N6)-threonylcarbamoyltransferase-complex-ATPase-subunit-type-1-TsaE	unknown	unknown	gnl\|CDD\|376771
NZ_CP029149.1\|WP_160224646.1\|1992164_1993157_+\|GTP-3',8-cyclase-MoaA	unknown	unknown	gnl\|CDD\|274250

Protein	Function_ID	Function_description	E-value
NZ_CP029149.1\|WP_120488948.1\|1991327_1991858_+\|Rieske-(2Fe-2S)-protein	gnl\|CDD\|239550	cd03467, Rieske, Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron oxygenase (RO) systems such as naphthalene and biphenyl dioxygenases, as well as in plant/cyanobacterial chloroplast b6f and mitochondrial cytochrome bc(1) complexes. The Rieske domain can be divided into two subdomains, with an incomplete six-stranded, antiparallel beta-barrel at one end, and an iron-sulfur cluster binding subdomain at the other. The Rieske iron-sulfur center contains a [2Fe-2S] cluster, which is involved in electron transfer, and is liganded to two histidine and two cysteine residues present in conserved sequences called Rieske motifs. In RO systems, the N-terminal Rieske domain of the alpha subunit acts as an electron shuttle that accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron in the alpha subunit C-terminal domain to be used for catalysis.	5.60693e-19
NZ_CP029149.1\|WP_120488937.1\|2007682_2009047_-\|MATE-family-efflux-transporter	gnl\|CDD\|240536	cd13131, MATE_NorM_like, Subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins similar to Vibrio cholerae NorM. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. This subfamily includes Vibrio cholerae NorM and functions most likely as a multidrug efflux pump, removing xenobiotics from the interior of the cell. The pump utilizes a cation gradient across the membrane to facilitate the export process. NorM appears to bind monovalent cations in an outward-facing conformation and may subsequently cycle through an inward-facing and outward-facing conformation to capture and release its substrate.	5.84596e-140
NZ_CP029149.1\|WP_120489692.1\|2010055_2011240_-\|sigma-54-dependent-Fis-family-transcriptional-regulator	gnl\|CDD\|225114	COG2204, AtoC, Response regulator containing CheY-like receiver, AAA-type ATPase, and DNA-binding domains [Signal transduction mechanisms].	5.88633e-169
NZ_CP029149.1\|WP_120488944.1\|1997233_1998043_-\|type-I-methionyl-aminopeptidase	gnl\|CDD\|238519	cd01086, MetAP1, Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and Peptidase M. Catalyzes release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.	1.04097e-127
NZ_CP029149.1\|WP_160224653.1\|2009574_2009985_+\|hypothetical-protein	gnl\|CDD\|224514	COG1598, COG1598, Predicted nuclease of the RNAse H fold, HicB family [General function prediction only].	0.00371509
NZ_CP029149.1\|WP_120488949.1\|1990732_1991308_+\|4Fe-4S-dicluster-domain-containing-protein	gnl\|CDD\|319891	cd16369, DMSOR_beta_like, uncharacterized subfamily of DMSO Reductase beta subunit family. This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.	2.18291e-89
NZ_CP029149.1\|WP_160224652.1\|2005406_2007257_-\|type-IIA-DNA-topoisomerase-subunit-B	gnl\|CDD\|235501	PRK05559, PRK05559, DNA topoisomerase IV subunit B; Reviewed.	0
NZ_CP029149.1\|WP_120488945.1\|1994036_1995377_+\|hypothetical-protein	gnl\|CDD\|238863	cd01825, SGNH_hydrolase_peri1, SGNH_peri1; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.	8.74991e-41
NZ_CP029149.1\|WP_160224648.1\|1999769_2000408_-\|rhomboid-family-intramembrane-serine-protease	gnl\|CDD\|366759	pfam01694, Rhomboid, Rhomboid family. This family contains integral membrane proteins that are related to Drosophila rhomboid protein. Members of this family are found in bacteria and eukaryotes. Rhomboid promotes the cleavage of the membrane-anchored TGF-alpha-like growth factor Spitz, allowing it to activate the Drosophila EGF receptor. Analysis has shown that Rhomboid-1 is an intramembrane serine protease (EC:3.4.21.105). Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite.	9.60063e-21
NZ_CP029149.1\|WP_120489693.1\|1998051_1998483_-\|hypothetical-protein	gnl\|CDD\|223319	COG0241, HisB, Histidinol phosphatase and related phosphatases [Amino acid transport and metabolism].	0.00115995
NZ_CP029149.1\|WP_160224649.1\|2000947_2003527_-\|DNA-gyrase/topoisomerase-IV-subunit-A	gnl\|CDD\|237192	PRK12758, PRK12758, DNA gyrase/topoisomerase IV subunit A.	0
NZ_CP029149.1\|WP_120488936.1\|2009349_2009532_+\|type-II-toxin-antitoxin-system-HicA-family-toxin	gnl\|CDD\|377942	pfam07927, HicA_toxin, HicA toxin of bacterial toxin-antitoxin,. HicA_toxin is a bacterial family of toxins that act as mRNA interferases. The antitoxin that neutralizes this is family HicB, pfam15919.	2.92364e-19
NZ_CP029149.1\|WP_160224650.1\|2003527_2004817_-\|TIGR00341-family-protein	gnl\|CDD\|377221	pfam04087, DUF389, Domain of unknown function (DUF389). Family of hypothetical bacterial proteins with an undetermined function.	7.32807e-61
NZ_CP029149.1\|WP_120488933.1\|2011818_2012196_-\|large-conductance-mechanosensitive-channel-protein-MscL	gnl\|CDD\|376605	pfam01741, MscL, Large-conductance mechanosensitive channel, MscL.	1.95247e-52
NZ_CP029149.1\|WP_160224647.1\|1998513_1999773_-\|CinA-family-nicotinamide-mononucleotide-deamidase-related-protein	gnl\|CDD\|234789	PRK00549, PRK00549, competence damage-inducible protein A; Provisional.	2.73395e-125
NZ_CP029149.1\|WP_120489694.1\|1995410_1997066_+\|MBOAT-family-protein	gnl\|CDD\|224610	COG1696, DltB, Predicted membrane protein involved in D-alanine export [Cell envelope biogenesis, outer membrane].	1.11655e-66
NZ_CP029149.1\|WP_120488934.1\|2011350_2011758_-\|tRNA-(adenosine(37)-N6)-threonylcarbamoyltransferase-complex-ATPase-subunit-type-1-TsaE	gnl\|CDD\|376771	pfam02367, TsaE, Threonylcarbamoyl adenosine biosynthesis protein TsaE. This family of proteins is involved in the synthesis of threonylcarbamoyl adenosine (t(6)A).	1.10107e-42
NZ_CP029149.1\|WP_160224646.1\|1992164_1993157_+\|GTP-3',8-cyclase-MoaA	gnl\|CDD\|274250	TIGR02666, Cyclic_pyranopterin_monophosphate_synthase, molybdenum cofactor biosynthesis protein A, bacterial. The model for this family describes molybdenum cofactor biosynthesis protein A, or MoaA, as found in bacteria. It does not include the family of probable functional equivalent proteins from the archaea. MoaA works together with MoaC to synthesize precursor Z from guanine. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin].	1.59409e-112

>NZ_CP029149.1|WP_160224648.1|1999769_2000408_-|rhomboid-family-intramembrane-serine-protease
MTLAGLVIIAITAIFSYRGFNEPLFFEQYKFSVGAIRQKREYYRLISSGFLHADWMHFIFNMLSLYFFQGIVSAAFGAGGFLIIYFGSMLLGNAFSLFLYKDQPWYSAIGASGAVSGVIFAAIALNPDGISVNFLPGWLFGTLYFSYSVYMLLRPKPWDNLGHSAHLGGAVFGLVYIFIAATQSAIENGLYLIIMLIPILYLAYILFKNKRR
>NZ_CP029149.1|WP_160224647.1|1998513_1999773_-|CinA-family-nicotinamide-mononucleotide-deamidase-related-protein
MSRPVQAVIICIGDELLSGNTLDTNSHYIANELRGIGIETKQIYTISDEAEIIEKTLKESLSLADIIISTGGLGPTKDDKTLEAYSRFFNRKLVFNDEVFAQLKIFLEKRGRAEILDLNRNQAMVLEGAEVLKNEHGTAPCQLIDDNDKLIFCLPGVPFEVKPLIKEKIIPLLKSRFGLHSILTAVVSVVGIPESALSHKIEDWETHLPKSLSLSYLPVGNRIKLRITAKGSTEIELQKQLKIEIQKLKSLLGTSIISEANDRIQDIVKDLLISRKMTISTAESCTGGAISKLLTSVSGSSAYFAGGVCTYSPEMKAKILGVAPSIIEKHTVVSAEVSQAMAKGCQQLFGTDISVSTTGVAGPNTDQYNNSIGLVYYSVRIGEKESTHKLFLPHLEREDFINFVSEKVLQTVVEEVLKS
>NZ_CP029149.1|WP_120489693.1|1998051_1998483_-|hypothetical-protein
MRSNKKLAIDFDGTIVEDAYPAIGKPKIFAFETLKKLQSEGYRLILWTYRSGKALDDAIDFCKKNGVEFYAVNSSFEGEVFDAETQSRKIDADLFIDDRNLGGFPGWGEIYNIINEKIEFRVEGREVLPYSKLKKEKKKGFFW
>NZ_CP029149.1|WP_120488944.1|1997233_1998043_-|type-I-methionyl-aminopeptidase
MIQLKTLEELYLIRESAQLVSKTLGMLAKEIKPGVTTLHLDNLAYEFIKDHNAEPGFLGLYDFPNTLCISPNEEVVHGIPNKKPLEEGDIISVDCGVYKNGFYGDHAYSFQVGEVSPEVKKLLKITKESLYKGIEQCIRGKRVGDISYAIQTYCEKEGYGVVRELVGHGVGRKMHEDPQVPNYGKRGSGKVLKDGIVLAIEPMINMGTEKVIFHQDGWTVTSQDNSPSAHFEHDVAIIKGKPVLLSTFKYVHEALGISSDEEEPFQYDW
>NZ_CP029149.1|WP_120489694.1|1995410_1997066_+|MBOAT-family-protein
MFLNLINSFNAEAFFSQFLYDPKNPLLFNNGFFVYFFFLFILLFYLLRHKPTARKYVFSCFSLYFFYKASGSFVLLVILSAVVNYLLSNAIYQLKEKRTKTLTLVVSIVINLGLLFYFKYTNFFISVANEIFNTGFNPLHILLPIGISFFTFENLSYTIDVYRGDFKPAHKFVDYLLFLSFFPKLMMGPIVRAHDFVPQLDKPYYINEKEFAKGFYLIISGLIKKLVISDYITLNLVDYIFDNPSLHTGLENLIALYGYAMVIYCDFSGYSDVAIGMALWLGFKIPPNFLSPYQSANITEFWRRWHISLSSWLKDYLYIPLGGNRNATFGSYLFVILFLIGSFMMLNHLFSLSYLYSGLITFGLLMIFVLPPLLKGNNKGIAANFNLLTTMLLGGFWHGASWNFIIWGALHGIALGIHKIWMMMTGKAFARFNNSKLYNFIMIVLTFHFACFCWIFFKAEDFDIALAMIRQIAFNFDFSVWMPFYENYKYVVWMIAFAMLIHFIPDDFIDKLVEKRNKFSLGLYILIFFAFLILYGFFKSSEQVMPIYLQF
>NZ_CP029149.1|WP_120488945.1|1994036_1995377_+|hypothetical-protein
MKNVNKKVISLTAICTIIYFVASVIFTAFNLSWEPFDKVNLISELIKSDGKKSTASAELKKKKDSLIASQNGKSEAKENFELYRKGNLITDFRESSSPALPSFAEKLHRLKKGEKVKIRIAYFGDSMIEGDLMTQTLRALLQGEYGGSGVGFLPINSNVAGFRQSATISVKGWQGTNFMDKAAQNLYISGYKYTGTGAGSYTDNTIKDSANTEKALIFGSGAASEVLVNGAAVQLSSTEKLNRKVLLKDSSNRIKISGNNVQTPLYGISFESESGIFVDNFSFRGITGVELNKIDEDFMRSVQKNNRYDLIVLQYGVNLLFKPKTTDYSFYSKMFSPVLSKMKTAFEGAEFLLISSADRAFKYNGEFKTAIGLPNLIETQALMAFENKIAFYNQFETMGGENSIVKWANEKPALANKDYIHPNHKGAEILAQRLFEAIQKDVAKKK
>NZ_CP029149.1|WP_160224646.1|1992164_1993157_+|GTP-3',8-cyclase-MoaA
MSIDLLDSFGRKHDYLRLSITDSCNFRCLYCMPDEPFSCSSIAELMSAEEIFNISKVFVEKFGIKKIRITGGEPLVRQDFKQIIELLSQLNVQIAITTNGVLLDRYFSLLEEKNIRDINISIDSLNRQKFKLLTKRDSLPKVWENILTGISKGFNIKLNAVIIDRVNTDDILPLAELSHRYPIEMRFIEFMPFNGNSWERNKVFPIRKMLSIIGEKYDYLKLFDAKNDTSKKYKLRIDSEGSFGFISTMTDSFCAGCNRIRLTSDGKMKNCLFGAEEFDLLSLYRQGQSIENAIKEGIWRKHKEKGGQFIHLQNIEEEKLANRSMIKIGG
>NZ_CP029149.1|WP_120488947.1|1991875_1992175_+|C4-dicarboxylate-ABC-transporter-permease
MAIRKKPIKKVTFRINEMLTFVIAIYIMFVALQMWLLFGTINKALYLYNTEIEVQPFATWSAIGSVVIFLCLVFFLRYIPRIPTGNIMKGDEKEEEYEY
>NZ_CP029149.1|WP_120488948.1|1991327_1991858_+|Rieske-(2Fe-2S)-protein
MSDNNNIPDWKADFPIKKREAGYVSRREFVKVVTLFSGLLAFANVFIPVFNYFHKKKVIKDYFVCFTDELEVGQQKTFYIDGDHRNPYMLIRMAKDKWKVFEQKCTHLSCGVIYKHDENLIECPCHHGFFDPENGEVLQGPPPRPLPQLGVVVKENRIYVEEYAYQKKKHHKAHHG
>NZ_CP029149.1|WP_120488949.1|1990732_1991308_+|4Fe-4S-dicluster-domain-containing-protein
MAEQFEKFNDMEFFLDMQRCIGCHSCEMACAECETNGETTMIHIHYVDRAETIQTTVQVCMHCDDPICANVCPADAITKDEFGIVHSADVSKCIGCANCVMSCPFGVPQIPDQNALLMMKCNMCYDRTSIGLKPMCATVCPSGALTFDTRENVAKKRPNSTPVNRFIFGEEVVTTKVNIMMPKGSKELKVF
>NZ_CP029149.1|WP_160224649.1|2000947_2003527_-|DNA-gyrase/topoisomerase-IV-subunit-A
MQENEHKEETLKKISGLYQDWFLDYASYVILDRAIPSVYDGFKPVQRRIMHSMRELEDGRYNKVANIVGNTMKYHPHGDASITDAMVQIGQKELLIDTQGNWGNIYTGDSAAAARYIEARLTPFALEVVFNPKTTEWVKSYDGRNNEPVDLPVKFPLLLAQGVEGIGVGLSTKILPHNFNELINASVAYLKGKSFELFPDFQTAGLLDVSEYNDGKRGGKVRVRAKITQQDKHTLIISELPFSKTTGDLIDSIIKANEKGKIKIKKIEDNTSDKVEIIIHLHNDVSPDKMIDALYAFTDCQVTLSPNACVIIGDKPVFTSVSEILKLNTDHTVSLLKKELEIELGELQESWHFASLERIFIENRIYHDIEEVKSWEEVLTTIDNGLKPHTGHLLRKVTTEDIIKLTEIRIKRISRFDLDKFRENIAALEDKIEKAKYNLEHLVQYAIDYYLSIQKKFGKERERRTELRIFDTIDATKVAVANIKFYANYSEGFVGTALRKDDYLFDCSDIDDIIVFRKDGTMQVVKVDQKTFVGKDILFVGIWKKNDSRTVYNMIYREGKLGPYYMKRFSVTSITRNTEYPLASDKKGSEVLYFSANPNGEAEIVSVILKPNARIRKQRLEIDFSELAIKGRNSRGNLVTKYAIKKIDLKEEGISTLAPRKIWFDDTVRRLNADGRGTLLGTFKGQDKILSITSKGEAKLLSFDLSNRFDDEYLILEKWKPQQPISCIYYDGEKKIYFIKRFLLENTPNLQTFMPSEHPKSFIEFVGTSDGCTAEIIFAKDKSGKEKDPETVNIDDFIAIKGIKAIGNQFVKDKIKSININIPEPDEEDLLTEDETSPHSSDEIPEEGIIGELFDEPTP
>NZ_CP029149.1|WP_160224650.1|2003527_2004817_-|TIGR00341-family-protein
MKRHNLFNLHEGEEKQDKVLQDVLKNISFKGANLWILACAIFIASIGLNVNSTAVIIGAMLISPLMGPIVGIGVALAIYDLTLLKKSGKNLLTATIVSLLVSAIYFTLSPFKEAQSEILARTSPNIYDVLIAFIGGIVGVISITRVEKGNPIPGVAIATALMPPLCTAGFGLATFNFKFFAGALYLYSINCFFIAIATFTIVKFLKYKPVSTQDEKFDRKVKYSIYILFTIMIVPSIFLAYRLISDNKYTKNVENFIKNEFTDKGHTVIYKKINKNETPKTIELVLLNQRMDSIEIQALNKKLADSYEIKDTKLLIKNNSSNLKSEILAEINKQNKDFSEKDIIIQNLTSELNEYKFDDRQLIKELRIIFPEVENISIGKLNSYEKDSRKQENTVIYQIKEKEKLDEEKLKKWLQTKLNDQNIRLINTK
>NZ_CP029149.1|WP_160224651.1|2004822_2005371_-|hypothetical-protein
MRLSNRKKEPLYNFINTLVIFSFAMSILIFFADRFELHTLGWKASLFLLINIVAFGLHFIRRKQIFEYDSDGEALNFRNYSIIPFLGREARDEFPKYKLISFDITDAVLFKRLHIKITSRKKNEIVLKYDISYLTSSEIRDLKLSLQRTIKANKENKENKENKENKENKENKENKENTDNEK
>NZ_CP029149.1|WP_160224652.1|2005406_2007257_-|type-IIA-DNA-topoisomerase-subunit-B
MSTKEQTNYSEENIRTLEWQEHVRLRPGMYIGKLGDGSSADDGIYILLKEVIDNSIDEFRMKAGKRIEIKLDEDKITVRDYGRGIPLGKVVDVVSKMNTGGKYDSKAFKKSVGLNGVGTKAVNALSTYFKVKSVREGQTKSAEFSKGNLTEDFPTAETNEKNGTEISFVPDAEIFVNYKFRNEYIERMLRNYAYLNPGLKIIFNGEAYYSEEGLKDLLTEEIGEEILYPIIHLKGEDIEVAITHSDKSQSETYFSFVNGQNTTQGGTHLNAFREAYVKTIREFFNKNFDASDVRKSIIAAISVNVEEPVFESQTKTKLGSNEMAPGGTSVRSFVIDFLKKELDNFLHKNPEIAEAINRKILISERERKELSGIQKLARERAKKVSLHNKKLRDCRQHYNDQKAQRKSETQIFITEGDSASGSITKSRDVETQAVFSLKGKPLNCYGLTKKVVYENEEFNLLQAALNIENSLEDLRYNQVIIATDADVDGMHIRLLMITFFLQFFPDVIKNGHLYILQTPLFRVRNKKETRYCYTEEERIKALSELGKNPEITRFKGLGEISPDEFKHFIGKDIRLEPVVIGKDQTIDQLLEFYMGKNTPDRQSFILENLVVEEALS
>NZ_CP029149.1|WP_120488937.1|2007682_2009047_-|MATE-family-efflux-transporter
MSFLNPVYTKQTLKLAIPVMLTQLGQASVNLFDNIIVGRLLGANALASVSLGNSVFFSVFVFALGISLAIPPLVSEANSQNNHSQINKVFSHGFVINLAIGILLAALLLLISPLMKYAQQPPEIIPDAMRFLNIMAISIIPFMIFQTMREVSEGLSYTIGVTVATVAANLINIALNYTFIEGLFGITPMGVAGSAYATLISRFFIIIFLYFIMRRESKTQKYLKEFSLKLEIFSKEMFRKMLKIGVPIAFQLFFEVSTFAGASFICGLVSATDVAAHQVAMTMVSFTYNLCVGFSVASTIMVGNKFGERDFLGARKIGVNNIKIAFIFMSLCCLIFILGKDILPTFYTKPGETNVVVLASMLLIIASLFQLSDGIQVVALGSLRGLQDVKIPSIFTFIAYWVITIPLGYYLCYVRGMGAVGMWIAFGVGLTISAVLLVRRFLILTSRSDFASAS
>NZ_CP029149.1|WP_120488936.1|2009349_2009532_+|type-II-toxin-antitoxin-system-HicA-family-toxin
MSSTELIRVIEDDGWYLVNVKGSHHHFKHQTKKGKVTIPHPKKDLPQGTINAILKQAGLK
>NZ_CP029149.1|WP_160224653.1|2009574_2009985_+|hypothetical-protein
MRKIKVTVRKENGVYWANTENIEGIVVADGNTFDEMKKNLQDAFDFHLEECEKDGDLGFVKKYKKGVEFVYEIELNGICKQLPEINLSELARRLKISPVMMRKYATGKTKASEKRLYEIQEGIRNIGKELVEVRLL
>NZ_CP029149.1|WP_120489692.1|2010055_2011240_-|sigma-54-dependent-Fis-family-transcriptional-regulator
MSQKVLIVEDEKTISGVLHSILSDELPEYDFTIAEDGLEGLKRVEKEEFSLVISDIKMPKLSGSDFLKQSLSINPDLTFIMISGHADIDTAVSCLKEGAYDFISKPIDINRLLTSVRNALDKGNLKKENKTLQSENKTLKKKVNKKYQMIGESEPLKKIQQMIDKVAASDARVLITGPNGAGKELVAHAIHSQSERSKGPIVEVNCAAIPSELIESELFGHIKGSFTGAIKDKSGKFEQANEGTIFLDEIGDMSLIAQAKVLRALQENKVSPVGSDKEIKVNVRVLAATNKDMKKEIAEGRFREDLYHRISVIEIYVPPLDERKEDIPLLVEHFAKLIADEQGNTPKKFSKEAIKKLQSFSWTGNIRELRNVVERLIILGGNPISEEDVVAFVR
>NZ_CP029149.1|WP_120488934.1|2011350_2011758_-|tRNA-(adenosine(37)-N6)-threonylcarbamoyltransferase-complex-ATPase-subunit-type-1-TsaE
MEFKIHRLEEWNEVIDALLPHIKHNILLMRGNLGAGKTTFTQFLLKKLGSADEVSSPTYAIVNEYHSPRGRVNHFDLYRMKSIEEVYDIGIEEYLDNAFLNIIEWAEIYEPALEGIPYHSLSIEVEEGVRRVVFE
>NZ_CP029149.1|WP_120488933.1|2011818_2012196_-|large-conductance-mechanosensitive-channel-protein-MscL
MSLIKEFKAFAFKGNVIDLAVGVIIGAAFGKIVSSLVDDVITPLLLNPVLKAAGADNIAKLSWNGVTYGNFLSSVISFFCIALVLFWLIKGANKLNKKPEEAPAPPAGPTQEELLAEIRDLLKNK

You can click texts colored in the table to view more detailed information

Click the colored protein region to show detailed information

Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity
NZ_CP029149_5	5.1\|988182\|39\|NZ_CP029149\|CRISPRCasFinder	988182-988220	39	NZ_CP029149.1	1567315-1567353	0	1.0
NZ_CP029149_4	4.2\|914019\|16\|NZ_CP029149\|CRISPRCasFinder	914019-914034	16	NZ_CP029149.1	1147056-1147071	1	0.938

1. spacer 5.1|988182|39|NZ_CP029149|CRISPRCasFinder matches to position: 1567315-1567353, mismatch: 0, identity: 1.0

atgccgtagtcggcactacacatatttacattcatctta	CRISPR spacer
atgccgtagtcggcactacacatatttacattcatctta	Protospacer
***************************************

2. spacer 4.2|914019|16|NZ_CP029149|CRISPRCasFinder matches to position: 1147056-1147071, mismatch: 1, identity: 0.938

tttaagtgctccacct	CRISPR spacer
tttaagtgctgcacct	Protospacer
********** *****

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP029149_9	9.13\|1505009\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505009-1505038	30	MF431738	Bacteriophage T5-like poul149, complete genome	86423-86452	5	0.833
NZ_CP029149_9	9.13\|1505009\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505009-1505038	30	MF431736	Bacteriophage T5-like chee130_1, complete genome	86423-86452	5	0.833
NZ_CP029149_9	9.13\|1505009\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505009-1505038	30	MF431737	Bacteriophage T5-like saus132, complete genome	86423-86452	5	0.833
NZ_CP029149_9	9.13\|1505009\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505009-1505038	30	MF431739	Bacteriophage T5-like chee158, complete genome	86423-86452	5	0.833
NZ_CP029149_9	9.13\|1505009\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505009-1505038	30	MF431740	Bacteriophage T5-like cott162, complete genome	86423-86452	5	0.833
NZ_CP029149_9	9.13\|1505009\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505009-1505038	30	MF431741	Bacteriophage T5-like saus176N, complete genome	86423-86452	5	0.833
NZ_CP029149_9	9.10\|1504778\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1504778-1504807	30	MT497081	Flavobacterium phage vB_Fsp_elemo11-5C, partial genome	58620-58649	6	0.8
NZ_CP029149_9	9.11\|1504855\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1504855-1504884	30	NC_015427	Clostridium botulinum BKT015925 plasmid p4BKT015925, complete sequence	8582-8611	6	0.8
NZ_CP029149_9	9.15\|1505163\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505163-1505192	30	MN855767	Bacteriophage sp. isolate 11, complete genome	24429-24458	6	0.8
NZ_CP029149_9	9.16\|1505240\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505240-1505269	30	NZ_CP015354	Bacillus thuringiensis strain MYBT18246 plasmid p120416, complete sequence	95015-95044	6	0.8
NZ_CP029149_9	9.19\|1505471\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505471-1505500	30	NC_004313	Salmonella phage ST64B, complete genome	34050-34079	6	0.8
NZ_CP029149_9	9.19\|1505471\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505471-1505500	30	KU927493	Salmonella phage 118970_sal3, complete genome	32198-32227	6	0.8
NZ_CP029149_9	9.19\|1505471\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505471-1505500	30	KU927493	Salmonella phage 118970_sal3, complete genome	71662-71691	6	0.8
NZ_CP029149_9	9.19\|1505471\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505471-1505500	30	AY055382	Salmonella typhimurium phage ST64B complete sequence	34050-34079	6	0.8
NZ_CP029149_9	9.20\|1505548\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505548-1505577	30	NC_009930	Acaryochloris marina MBIC11017 plasmid pREB5, complete sequence	59604-59633	6	0.8
NZ_CP029149_9	9.6\|1504470\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1504470-1504499	30	NZ_CP016750	Lactococcus lactis subsp. cremoris strain JM1 plasmid pJM1D, complete sequence	8993-9022	7	0.767
NZ_CP029149_9	9.7\|1504547\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1504547-1504576	30	MN657126	Psychrobacter sp. strain ANT_P59 plasmid pA59P3, complete sequence	1482-1511	7	0.767
NZ_CP029149_9	9.7\|1504547\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1504547-1504576	30	KP211958	Cyanophage P-TIM40, complete genome	42098-42127	7	0.767
NZ_CP029149_9	9.8\|1504624\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1504624-1504653	30	NZ_CP010903	Acinetobacter nosocomialis strain 6411 plasmid p6411-66.409kb, complete sequence	62223-62252	7	0.767
NZ_CP029149_9	9.13\|1505009\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505009-1505038	30	LR214966	Mycoplasma fermentans strain NCTC10117 genome assembly, plasmid: 12	20399-20428	7	0.767
NZ_CP029149_9	9.13\|1505009\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505009-1505038	30	LR214966	Mycoplasma fermentans strain NCTC10117 genome assembly, plasmid: 12	62870-62899	7	0.767
NZ_CP029149_9	9.13\|1505009\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505009-1505038	30	LR214967	Mycoplasma fermentans strain NCTC10117 genome assembly, plasmid: 13	21685-21714	7	0.767
NZ_CP029149_9	9.13\|1505009\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505009-1505038	30	LR214967	Mycoplasma fermentans strain NCTC10117 genome assembly, plasmid: 13	26945-26974	7	0.767
NZ_CP029149_9	9.13\|1505009\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505009-1505038	30	MN693882	Marine virus AFVG_250M174, complete genome	9406-9435	7	0.767
NZ_CP029149_9	9.13\|1505009\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505009-1505038	30	MN693875	Marine virus AFVG_250M965, complete genome	9428-9457	7	0.767
NZ_CP029149_9	9.13\|1505009\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505009-1505038	30	MN694418	Marine virus AFVG_250M966, complete genome	9414-9443	7	0.767
NZ_CP029149_9	9.13\|1505009\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505009-1505038	30	MN694481	Marine virus AFVG_250M175, complete genome	9392-9421	7	0.767
NZ_CP029149_9	9.13\|1505009\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505009-1505038	30	NZ_CP026601	Clostridiaceae bacterium 14S0207 plasmid unnamed1, complete sequence	133246-133275	7	0.767
NZ_CP029149_9	9.20\|1505548\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505548-1505577	30	NZ_LR215032	Mycoplasma gallopavonis strain NCTC10186 plasmid 2	125736-125765	7	0.767
NZ_CP029149_9	9.22\|1505702\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505702-1505731	30	MN693605	Marine virus AFVG_25M414, complete genome	25503-25532	7	0.767
NZ_CP029149_9	9.25\|1505933\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505933-1505962	30	NZ_CP045607	Bacillus cereus strain SB1 plasmid p1, complete sequence	77329-77358	7	0.767
NZ_CP029149_9	9.25\|1505933\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505933-1505962	30	MN693728	Marine virus AFVG_250M561, complete genome	41608-41637	7	0.767
NZ_CP029149_9	9.1\|1504085\|30\|NZ_CP029149\|PILER-CR,CRISPRCasFinder	1504085-1504114	30	NC_016585	Azospirillum lipoferum 4B plasmid AZO_p1, complete sequence	842794-842823	8	0.733
NZ_CP029149_9	9.4\|1504316\|30\|NZ_CP029149\|PILER-CR,CRISPRCasFinder	1504316-1504345	30	MG983840	Escherichia phage myPSH1131, complete genome	29099-29128	8	0.733
NZ_CP029149_9	9.4\|1504316\|30\|NZ_CP029149\|PILER-CR,CRISPRCasFinder	1504316-1504345	30	MG983840	Escherichia phage myPSH1131, complete genome	34775-34804	8	0.733
NZ_CP029149_9	9.4\|1504316\|30\|NZ_CP029149\|PILER-CR,CRISPRCasFinder	1504316-1504345	30	MG976803	Escherichia phage myPSH2311, complete genome	30845-30874	8	0.733
NZ_CP029149_9	9.4\|1504316\|30\|NZ_CP029149\|PILER-CR,CRISPRCasFinder	1504316-1504345	30	EU330206	Enterobacteria phage phiEco32, complete genome	33691-33720	8	0.733
NZ_CP029149_9	9.4\|1504316\|30\|NZ_CP029149\|PILER-CR,CRISPRCasFinder	1504316-1504345	30	MN508615	UNVERIFIED: Escherichia phage ES17, complete genome	39964-39993	8	0.733
NZ_CP029149_9	9.4\|1504316\|30\|NZ_CP029149\|PILER-CR,CRISPRCasFinder	1504316-1504345	30	MT446386	UNVERIFIED: Escherichia virus TH06, complete genome	15066-15095	8	0.733
NZ_CP029149_9	9.6\|1504470\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1504470-1504499	30	MT773554	Myoviridae sp. isolate BML_2 genomic sequence	153660-153689	8	0.733
NZ_CP029149_9	9.6\|1504470\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1504470-1504499	30	MT773554	Myoviridae sp. isolate BML_2 genomic sequence	156949-156978	8	0.733
NZ_CP029149_9	9.8\|1504624\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1504624-1504653	30	NZ_LR215032	Mycoplasma gallopavonis strain NCTC10186 plasmid 2	145625-145654	8	0.733
NZ_CP029149_9	9.13\|1505009\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505009-1505038	30	NC_015907	Borreliella bissettii DN127 plasmid cp26, complete sequence	22528-22557	8	0.733
NZ_CP029149_9	9.13\|1505009\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505009-1505038	30	NZ_CP015797	Borrelia mayonii strain MN14-1539 plasmid cp26, complete sequence	22899-22928	8	0.733
NZ_CP029149_9	9.13\|1505009\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505009-1505038	30	NZ_CP015781	Borrelia mayonii strain MN14-1420 plasmid cp26, complete sequence	22925-22954	8	0.733
NZ_CP029149_9	9.13\|1505009\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505009-1505038	30	NZ_CP041688	Chryseobacterium sp. SNU WT5 plasmid unnamed1, complete sequence	47167-47196	8	0.733
NZ_CP029149_9	9.13\|1505009\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505009-1505038	30	NZ_CP006906	Clostridium baratii str. Sullivan plasmid pCBJ, complete sequence	88513-88542	8	0.733
NZ_CP029149_9	9.13\|1505009\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505009-1505038	30	MN694628	Marine virus AFVG_250M527, complete genome	18024-18053	8	0.733
NZ_CP029149_9	9.20\|1505548\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505548-1505577	30	MN693558	Marine virus AFVG_25M213, complete genome	4761-4790	8	0.733
NZ_CP029149_9	9.24\|1505856\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505856-1505885	30	MF448564	Lactococcus phage 62601, complete genome	18991-19020	8	0.733
NZ_CP029149_9	9.24\|1505856\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505856-1505885	30	NC_049408	Lactococcus phage 62605, complete genome	18787-18816	8	0.733
NZ_CP029149_9	9.25\|1505933\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505933-1505962	30	MT074139	Bacteroides phage DAC19, complete genome	104583-104612	8	0.733
NZ_CP029149_9	9.25\|1505933\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505933-1505962	30	MT074140	Bacteroides phage DAC20, complete genome	104582-104611	8	0.733
NZ_CP029149_9	9.25\|1505933\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505933-1505962	30	NZ_CP010684	Phaeobacter piscinae strain P14 plasmid pP14_c, complete sequence	43116-43145	8	0.733
NZ_CP029149_9	9.7\|1504547\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1504547-1504576	30	NZ_CP049890	Jeotgalibaca porci strain CCUG 69148 plasmid p_unnamed1, complete sequence	2331-2360	9	0.7
NZ_CP029149_9	9.12\|1504932\|30\|NZ_CP029149\|CRISPRCasFinder	1504932-1504961	30	NZ_CP015501	Klebsiella pneumoniae strain SKGH01 plasmid unnamed 1, complete sequence	258752-258781	9	0.7
NZ_CP029149_9	9.12\|1504932\|30\|NZ_CP029149\|CRISPRCasFinder	1504932-1504961	30	NZ_LN824134	Klebsiella pneumoniae genome assembly MS6671.v1, plasmid : _Plasmid_A_Kpneumoniae_MS6671	47778-47807	9	0.7
NZ_CP029149_9	9.12\|1504932\|30\|NZ_CP029149\|CRISPRCasFinder	1504932-1504961	30	NZ_CP031818	Klebsiella pneumoniae strain INF235-sc-2280127 plasmid unnamed1, complete sequence	263828-263857	9	0.7
NZ_CP029149_9	9.12\|1504932\|30\|NZ_CP029149\|CRISPRCasFinder	1504932-1504961	30	NZ_CP024507	Klebsiella pneumoniae strain KSB2_1B plasmid unnamed1, complete sequence	21025-21054	9	0.7
NZ_CP029149_9	9.13\|1505009\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505009-1505038	30	MN693046	Marine virus AFVG_25M413, complete genome	46476-46505	9	0.7
NZ_CP029149_9	9.13\|1505009\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505009-1505038	30	MN693008	Marine virus AFVG_117M9, complete genome	46446-46475	9	0.7
NZ_CP029149_9	9.21\|1505625\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505625-1505654	30	AP014693	Ralstonia phage RSL2 DNA, complete sequence	27713-27742	9	0.7
NZ_CP029149_9	9.22\|1505702\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505702-1505731	30	MN694678	Marine virus AFVG_250M509, complete genome	39182-39211	9	0.7
NZ_CP029149_9	9.25\|1505933\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505933-1505962	30	NZ_CP014284	Bacillus thuringiensis strain Bt185 plasmid pBT1850294, complete sequence	279208-279237	9	0.7
NZ_CP029149_9	9.25\|1505933\|30\|NZ_CP029149\|CRISPRCasFinder,PILER-CR	1505933-1505962	30	NZ_CP032609	Bacillus thuringiensis strain QZL38 plasmid p.2, complete sequence	73049-73078	9	0.7

1. spacer 9.13|1505009|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to MF431738 (Bacteriophage T5-like poul149, complete genome) position: , mismatch: 5, identity: 0.833

attaaaaaaataattgaggat----ataagccct	CRISPR spacer
attaaagaaataattgaggataatgataag----	Protospacer
******.**************    *****

2. spacer 9.13|1505009|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to MF431736 (Bacteriophage T5-like chee130_1, complete genome) position: , mismatch: 5, identity: 0.833

attaaaaaaataattgaggat----ataagccct	CRISPR spacer
attaaagaaataattgaggataatgataag----	Protospacer
******.**************    *****

3. spacer 9.13|1505009|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to MF431737 (Bacteriophage T5-like saus132, complete genome) position: , mismatch: 5, identity: 0.833

attaaaaaaataattgaggat----ataagccct	CRISPR spacer
attaaagaaataattgaggataatgataag----	Protospacer
******.**************    *****

4. spacer 9.13|1505009|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to MF431739 (Bacteriophage T5-like chee158, complete genome) position: , mismatch: 5, identity: 0.833

attaaaaaaataattgaggat----ataagccct	CRISPR spacer
attaaagaaataattgaggataatgataag----	Protospacer
******.**************    *****

5. spacer 9.13|1505009|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to MF431740 (Bacteriophage T5-like cott162, complete genome) position: , mismatch: 5, identity: 0.833

attaaaaaaataattgaggat----ataagccct	CRISPR spacer
attaaagaaataattgaggataatgataag----	Protospacer
******.**************    *****

6. spacer 9.13|1505009|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to MF431741 (Bacteriophage T5-like saus176N, complete genome) position: , mismatch: 5, identity: 0.833

attaaaaaaataattgaggat----ataagccct	CRISPR spacer
attaaagaaataattgaggataatgataag----	Protospacer
******.**************    *****

7. spacer 9.10|1504778|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to MT497081 (Flavobacterium phage vB_Fsp_elemo11-5C, partial genome) position: , mismatch: 6, identity: 0.8

tgctctgagtttatcaaattcaactctaac	CRISPR spacer
tgcatcaagtttatcaaattcacctttaac	Protospacer
*** ...*************** **.****

8. spacer 9.11|1504855|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to NC_015427 (Clostridium botulinum BKT015925 plasmid p4BKT015925, complete sequence) position: , mismatch: 6, identity: 0.8

---caattcatttcagatgctattagagtagag	CRISPR spacer
atgaaat---tttcagatgctattagattagat	Protospacer
    ***   ***************** ****

9. spacer 9.15|1505163|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to MN855767 (Bacteriophage sp. isolate 11, complete genome) position: , mismatch: 6, identity: 0.8

-acctatctaaatgctttaatgaggcaatgg	CRISPR spacer
catct-cttaaattcttgaatgaggcaatgg	Protospacer
 *.** ..***** *** *************

10. spacer 9.16|1505240|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to NZ_CP015354 (Bacillus thuringiensis strain MYBT18246 plasmid p120416, complete sequence) position: , mismatch: 6, identity: 0.8

attgttttaattgatgcgtcaaatatacgc	CRISPR spacer
attgttttaattgatttgtcaaaattgagc	Protospacer
*************** .******  *. **

11. spacer 9.19|1505471|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to NC_004313 (Salmonella phage ST64B, complete genome) position: , mismatch: 6, identity: 0.8

gggagattctgctgggttttacagcaaaag	CRISPR spacer
gggtgattctgctgggttttatgcgcaaag	Protospacer
*** *****************..   ****

12. spacer 9.19|1505471|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to KU927493 (Salmonella phage 118970_sal3, complete genome) position: , mismatch: 6, identity: 0.8

gggagattctgctgggttttacagcaaaag	CRISPR spacer
gggtgattctgctgggttttatgcgcaaag	Protospacer
*** *****************..   ****

13. spacer 9.19|1505471|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to KU927493 (Salmonella phage 118970_sal3, complete genome) position: , mismatch: 6, identity: 0.8

gggagattctgctgggttttacagcaaaag	CRISPR spacer
gggtgattctgctgggttttatgcgcaaag	Protospacer
*** *****************..   ****

14. spacer 9.19|1505471|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to AY055382 (Salmonella typhimurium phage ST64B complete sequence) position: , mismatch: 6, identity: 0.8

gggagattctgctgggttttacagcaaaag	CRISPR spacer
gggtgattctgctgggttttatgcgcaaag	Protospacer
*** *****************..   ****

15. spacer 9.20|1505548|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to NC_009930 (Acaryochloris marina MBIC11017 plasmid pREB5, complete sequence) position: , mismatch: 6, identity: 0.8

acacaataattttatgaatacaacaacatt	CRISPR spacer
aatcaatatttttatgaatacaacagaata	Protospacer
*  ***** ****************. **

16. spacer 9.6|1504470|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to NZ_CP016750 (Lactococcus lactis subsp. cremoris strain JM1 plasmid pJM1D, complete sequence) position: , mismatch: 7, identity: 0.767

actccgttttcatcatagtaatctgttacg	CRISPR spacer
tttactttttcttcatagtaatctgttgca	Protospacer
 .* * ***** ***************.*.

17. spacer 9.7|1504547|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to MN657126 (Psychrobacter sp. strain ANT_P59 plasmid pA59P3, complete sequence) position: , mismatch: 7, identity: 0.767

gctggatctattattttgatggtagtgatt	CRISPR spacer
tggggatgtattattttgacggtagtggtg	Protospacer
   **** ***********.*******.*

18. spacer 9.7|1504547|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to KP211958 (Cyanophage P-TIM40, complete genome) position: , mismatch: 7, identity: 0.767

gctggatctattattttgatggtagtgatt	CRISPR spacer
caggtatctattactttgatgatagtgatg	Protospacer
   * ********.*******.*******

19. spacer 9.8|1504624|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to NZ_CP010903 (Acinetobacter nosocomialis strain 6411 plasmid p6411-66.409kb, complete sequence) position: , mismatch: 7, identity: 0.767

agttctaaatgtaacatttgaattactttt	CRISPR spacer
aaattataatgtaatatttgaactactttt	Protospacer
*. *.  *******.*******.*******

20. spacer 9.13|1505009|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to LR214966 (Mycoplasma fermentans strain NCTC10117 genome assembly, plasmid: 12) position: , mismatch: 7, identity: 0.767

attaaaaaaataattgaggatataagccct	CRISPR spacer
gttaaaaaaataattgaagatattaataat	Protospacer
.****************.***** *..  *

21. spacer 9.13|1505009|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to LR214966 (Mycoplasma fermentans strain NCTC10117 genome assembly, plasmid: 12) position: , mismatch: 7, identity: 0.767

attaaaaaaataattgaggatataagccct	CRISPR spacer
gttaaaaaaataattgaagatattaataat	Protospacer
.****************.***** *..  *

22. spacer 9.13|1505009|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to LR214967 (Mycoplasma fermentans strain NCTC10117 genome assembly, plasmid: 13) position: , mismatch: 7, identity: 0.767

attaaaaaaataattgaggatataagccct	CRISPR spacer
gttaaaaaaataattgaagatattaataat	Protospacer
.****************.***** *..  *

23. spacer 9.13|1505009|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to LR214967 (Mycoplasma fermentans strain NCTC10117 genome assembly, plasmid: 13) position: , mismatch: 7, identity: 0.767

attaaaaaaataattgaggatataagccct	CRISPR spacer
gttaaaaaaataattgaagatattaataat	Protospacer
.****************.***** *..  *

24. spacer 9.13|1505009|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to MN693882 (Marine virus AFVG_250M174, complete genome) position: , mismatch: 7, identity: 0.767

attaaaaaaataattgaggatataagccct	CRISPR spacer
attaacaaaataattgatgatatagaaagt	Protospacer
***** *********** ******..   *

25. spacer 9.13|1505009|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to MN693875 (Marine virus AFVG_250M965, complete genome) position: , mismatch: 7, identity: 0.767

attaaaaaaataattgaggatataagccct	CRISPR spacer
attaataaaataattgatgatatagaaagt	Protospacer
***** *********** ******..   *

26. spacer 9.13|1505009|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to MN694418 (Marine virus AFVG_250M966, complete genome) position: , mismatch: 7, identity: 0.767

attaaaaaaataattgaggatataagccct	CRISPR spacer
attaataaaataattgatgatatagaaagt	Protospacer
***** *********** ******..   *

27. spacer 9.13|1505009|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to MN694481 (Marine virus AFVG_250M175, complete genome) position: , mismatch: 7, identity: 0.767

attaaaaaaataattgaggatataagccct	CRISPR spacer
attaacaaaataattgatgatatagaaagt	Protospacer
***** *********** ******..   *

28. spacer 9.13|1505009|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to NZ_CP026601 (Clostridiaceae bacterium 14S0207 plasmid unnamed1, complete sequence) position: , mismatch: 7, identity: 0.767

attaaaaaaataattgaggatataagccct	CRISPR spacer
ggtggaaaaataattgatgatataagaact	Protospacer
. *..************ ********  **

29. spacer 9.20|1505548|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to NZ_LR215032 (Mycoplasma gallopavonis strain NCTC10186 plasmid 2) position: , mismatch: 7, identity: 0.767

acacaataattttatgaatacaacaacatt	CRISPR spacer
aattaataattctttgaatacaacaacttc	Protospacer
*  .*******.* ************* *.

30. spacer 9.22|1505702|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to MN693605 (Marine virus AFVG_25M414, complete genome) position: , mismatch: 7, identity: 0.767

actgctcaactcgatagcttcatctatttt	CRISPR spacer
tctttgctcctcgatagcttcatctagttt	Protospacer
 ** . *  ***************** ***

31. spacer 9.25|1505933|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to NZ_CP045607 (Bacillus cereus strain SB1 plasmid p1, complete sequence) position: , mismatch: 7, identity: 0.767

taaatgaaaagagcataacaataaaagaat	CRISPR spacer
ttaatgaaaataccataacaataaaaatga	Protospacer
* ******** * *************. .

32. spacer 9.25|1505933|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to MN693728 (Marine virus AFVG_250M561, complete genome) position: , mismatch: 7, identity: 0.767

taaatgaaaagagcataacaataaaagaat	CRISPR spacer
gagaataaatgagcagaacaataaaagaaa	Protospacer
 *.*  *** ***** *************

33. spacer 9.1|1504085|30|NZ_CP029149|PILER-CR,CRISPRCasFinder matches to NC_016585 (Azospirillum lipoferum 4B plasmid AZO_p1, complete sequence) position: , mismatch: 8, identity: 0.733

tgatcgggtgtcaggcatgaggcggtcgat	CRISPR spacer
gcatcgggcgtcaggcatgagccggttccc	Protospacer
  ******.************ ****.  .

34. spacer 9.4|1504316|30|NZ_CP029149|PILER-CR,CRISPRCasFinder matches to MG983840 (Escherichia phage myPSH1131, complete genome) position: , mismatch: 8, identity: 0.733

tgcgtcaaagatgagtttgaggagcccatt	CRISPR spacer
ttcgtcagagatgagttggaggagctatcc	Protospacer
* *****.********* *******.  ..

35. spacer 9.4|1504316|30|NZ_CP029149|PILER-CR,CRISPRCasFinder matches to MG983840 (Escherichia phage myPSH1131, complete genome) position: , mismatch: 8, identity: 0.733

tgcgtcaaagatgagtttgaggagcccatt	CRISPR spacer
ttcgtcagagatgagttggaggagctatcc	Protospacer
* *****.********* *******.  ..

36. spacer 9.4|1504316|30|NZ_CP029149|PILER-CR,CRISPRCasFinder matches to MG976803 (Escherichia phage myPSH2311, complete genome) position: , mismatch: 8, identity: 0.733

tgcgtcaaagatgagtttgaggagcccatt	CRISPR spacer
ttcgtcagagatgagttggaggagctatcc	Protospacer
* *****.********* *******.  ..

37. spacer 9.4|1504316|30|NZ_CP029149|PILER-CR,CRISPRCasFinder matches to EU330206 (Enterobacteria phage phiEco32, complete genome) position: , mismatch: 8, identity: 0.733

tgcgtcaaagatgagtttgaggagcccatt	CRISPR spacer
ttcgtcagagatgagttggaggagctatcc	Protospacer
* *****.********* *******.  ..

38. spacer 9.4|1504316|30|NZ_CP029149|PILER-CR,CRISPRCasFinder matches to MN508615 (UNVERIFIED: Escherichia phage ES17, complete genome) position: , mismatch: 8, identity: 0.733

tgcgtcaaagatgagtttgaggagcccatt	CRISPR spacer
ttcgtcagagatgagttggaggagctatcc	Protospacer
* *****.********* *******.  ..

39. spacer 9.4|1504316|30|NZ_CP029149|PILER-CR,CRISPRCasFinder matches to MT446386 (UNVERIFIED: Escherichia virus TH06, complete genome) position: , mismatch: 8, identity: 0.733

tgcgtcaaagatgagtttgaggagcccatt	CRISPR spacer
ttcgtcagagatgagttggaggagctatcc	Protospacer
* *****.********* *******.  ..

40. spacer 9.6|1504470|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to MT773554 (Myoviridae sp. isolate BML_2 genomic sequence) position: , mismatch: 8, identity: 0.733

actccgttttcatcatagtaatctgttacg	CRISPR spacer
ccagagttttgataatagtaatctgttaga	Protospacer
 *   ***** ** ************** .

41. spacer 9.6|1504470|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to MT773554 (Myoviridae sp. isolate BML_2 genomic sequence) position: , mismatch: 8, identity: 0.733

actccgttttcatcatagtaatctgttacg	CRISPR spacer
ccagggttttgataatagtaatctgttaga	Protospacer
 *   ***** ** ************** .

42. spacer 9.8|1504624|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to NZ_LR215032 (Mycoplasma gallopavonis strain NCTC10186 plasmid 2) position: , mismatch: 8, identity: 0.733

agttctaaatgtaacatttgaattactttt	CRISPR spacer
gattgtaaatttaacatttgaattaaagtg	Protospacer
..** ***** **************   *

43. spacer 9.13|1505009|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to NC_015907 (Borreliella bissettii DN127 plasmid cp26, complete sequence) position: , mismatch: 8, identity: 0.733

attaaaaaaataattgaggatataagccct	CRISPR spacer
attaaaaaaatatttgaggatctagagtaa	Protospacer
************ ******** **.. .

44. spacer 9.13|1505009|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to NZ_CP015797 (Borrelia mayonii strain MN14-1539 plasmid cp26, complete sequence) position: , mismatch: 8, identity: 0.733

attaaaaaaataattgaggatataagccct	CRISPR spacer
attaaaaaaatatttgaggatctagattaa	Protospacer
************ ******** **....

45. spacer 9.13|1505009|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to NZ_CP015781 (Borrelia mayonii strain MN14-1420 plasmid cp26, complete sequence) position: , mismatch: 8, identity: 0.733

attaaaaaaataattgaggatataagccct	CRISPR spacer
attaaaaaaatatttgaggatctagattaa	Protospacer
************ ******** **....

46. spacer 9.13|1505009|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to NZ_CP041688 (Chryseobacterium sp. SNU WT5 plasmid unnamed1, complete sequence) position: , mismatch: 8, identity: 0.733

attaaaaaaataattgaggatataagccct	CRISPR spacer
gttaataaaataattgagaatataaaaaac	Protospacer
.**** ************.******.   .

47. spacer 9.13|1505009|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to NZ_CP006906 (Clostridium baratii str. Sullivan plasmid pCBJ, complete sequence) position: , mismatch: 8, identity: 0.733

attaaaaaaataattgaggatataagccct	CRISPR spacer
attaaaaaaatgatagaggatattgatttt	Protospacer
***********.** ******** .....*

48. spacer 9.13|1505009|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to MN694628 (Marine virus AFVG_250M527, complete genome) position: , mismatch: 8, identity: 0.733

attaaaaaaataattgaggatataagccct	CRISPR spacer
attaaaaaaataggtgaggatattgtagat	Protospacer
************. ********* .    *

49. spacer 9.20|1505548|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to MN693558 (Marine virus AFVG_25M213, complete genome) position: , mismatch: 8, identity: 0.733

acacaataattttatgaatacaacaacatt	CRISPR spacer
gagcaataatattatgaatacaacattaaa	Protospacer
. .******* ************** .*

50. spacer 9.24|1505856|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to MF448564 (Lactococcus phage 62601, complete genome) position: , mismatch: 8, identity: 0.733

aatacttaaaaggcactaaatcaccgtata	CRISPR spacer
ctaacttaaaagccactaaatcacgtttga	Protospacer
   ********* ***********  *  *

51. spacer 9.24|1505856|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to NC_049408 (Lactococcus phage 62605, complete genome) position: , mismatch: 8, identity: 0.733

aatacttaaaaggcactaaatcaccgtata	CRISPR spacer
ctaacttaaaagtcactaaatcacgtttga	Protospacer
   ********* ***********  *  *

52. spacer 9.25|1505933|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to MT074139 (Bacteroides phage DAC19, complete genome) position: , mismatch: 8, identity: 0.733

taaatgaaaagagcataacaataaaagaat	CRISPR spacer
tttcaccaaatagcataaaaataaaagaat	Protospacer
*      *** ******* ***********

53. spacer 9.25|1505933|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to MT074140 (Bacteroides phage DAC20, complete genome) position: , mismatch: 8, identity: 0.733

taaatgaaaagagcataacaataaaagaat	CRISPR spacer
tttcaccaaatagcataaaaataaaagaat	Protospacer
*      *** ******* ***********

54. spacer 9.25|1505933|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to NZ_CP010684 (Phaeobacter piscinae strain P14 plasmid pP14_c, complete sequence) position: , mismatch: 8, identity: 0.733

taaatgaaaagagcataacaataaaagaat	CRISPR spacer
agaacgaaaagagcataacaatgaattttt	Protospacer
 .**.*****************.**    *

55. spacer 9.7|1504547|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to NZ_CP049890 (Jeotgalibaca porci strain CCUG 69148 plasmid p_unnamed1, complete sequence) position: , mismatch: 9, identity: 0.7

gctggatctattattttgatggtagtgatt	CRISPR spacer
aaaatttctagtattttgatggtagtgtat	Protospacer
.  .  **** ****************  *

56. spacer 9.12|1504932|30|NZ_CP029149|CRISPRCasFinder matches to NZ_CP015501 (Klebsiella pneumoniae strain SKGH01 plasmid unnamed 1, complete sequence) position: , mismatch: 9, identity: 0.7

taattctgagataatagagctgttactccg	CRISPR spacer
acgcacgttgataatagagctgttaatccg	Protospacer
  .. *   **************** ****

57. spacer 9.12|1504932|30|NZ_CP029149|CRISPRCasFinder matches to NZ_LN824134 (Klebsiella pneumoniae genome assembly MS6671.v1, plasmid : _Plasmid_A_Kpneumoniae_MS6671) position: , mismatch: 9, identity: 0.7

taattctgagataatagagctgttactccg	CRISPR spacer
acgcacgttgataatagagctgttaatccg	Protospacer
  .. *   **************** ****

58. spacer 9.12|1504932|30|NZ_CP029149|CRISPRCasFinder matches to NZ_CP031818 (Klebsiella pneumoniae strain INF235-sc-2280127 plasmid unnamed1, complete sequence) position: , mismatch: 9, identity: 0.7

taattctgagataatagagctgttactccg	CRISPR spacer
acgcacgttgataatagagctgttaatccg	Protospacer
  .. *   **************** ****

59. spacer 9.12|1504932|30|NZ_CP029149|CRISPRCasFinder matches to NZ_CP024507 (Klebsiella pneumoniae strain KSB2_1B plasmid unnamed1, complete sequence) position: , mismatch: 9, identity: 0.7

taattctgagataatagagctgttactccg	CRISPR spacer
acgcacgttgataatagagctgttaatccg	Protospacer
  .. *   **************** ****

60. spacer 9.13|1505009|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to MN693046 (Marine virus AFVG_25M413, complete genome) position: , mismatch: 9, identity: 0.7

attaaaaaaataattgaggatataagccct	CRISPR spacer
agaaaaaaaataattaaggatatatttatc	Protospacer
*  ************.********  . ..

61. spacer 9.13|1505009|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to MN693008 (Marine virus AFVG_117M9, complete genome) position: , mismatch: 9, identity: 0.7

attaaaaaaataattgaggatataagccct	CRISPR spacer
aagaaaaaaataattaaggatatatttatc	Protospacer
*  ************.********  . ..

62. spacer 9.21|1505625|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to AP014693 (Ralstonia phage RSL2 DNA, complete sequence) position: , mismatch: 9, identity: 0.7

ttttaacggctttggtctcggcattcacaa	CRISPR spacer
gcgatacggctttgttcccggcattcacct	Protospacer
 .   ********* **.**********

63. spacer 9.22|1505702|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to MN694678 (Marine virus AFVG_250M509, complete genome) position: , mismatch: 9, identity: 0.7

actgctcaactcgatagcttcatctatttt	CRISPR spacer
taaagccaactcaatagcttgatctatttc	Protospacer
   . .******.******* ********.

64. spacer 9.25|1505933|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to NZ_CP014284 (Bacillus thuringiensis strain Bt185 plasmid pBT1850294, complete sequence) position: , mismatch: 9, identity: 0.7

taaatgaaaagagcataacaataaaagaat	CRISPR spacer
aaaatgaaaagagtataacaatttgtataa	Protospacer
 ************.********  . . *

65. spacer 9.25|1505933|30|NZ_CP029149|CRISPRCasFinder,PILER-CR matches to NZ_CP032609 (Bacillus thuringiensis strain QZL38 plasmid p.2, complete sequence) position: , mismatch: 9, identity: 0.7

taaatgaaaagagcataacaataaaagaat	CRISPR spacer
aaaatgaaaagagtataacaatttgtataa	Protospacer
 ************.********  . . *

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

835956 : 846930

Staphylococcus_phage(16.67%)

integrase

attL 837667:837685|attR 851908:851926

The bacterium proteins that are colored denote the protein is present at specific phage-related keywords (such as 'capsid', 'head', 'integrase', 'plate', 'tail', 'fiber', 'coat', 'transposase', 'portal', 'terminase', 'protease' or 'lysin' and 'tRNA')

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_120488300.1\|835956_837558_-	phosphoenolpyruvate carboxykinase (ATP)	A0A2H4PQN1	Staphylococcus_phage	1.7e-140	52.1
837667:837685	attL	NA	NA	NA	NA
WP_160224035.1\|837952_839176_-	cysteine desulfurase	Q2XUY6	environmental_halophage	4.0e-94	42.2
WP_120488298.1\|839306_839852_-	transcription termination/antitermination factor NusG	A0A291AUL3	Sinorhizobium_phage	9.1e-06	28.1
WP_120488297.1\|839868_840075_-	preprotein translocase subunit SecE	NA	NA	NA	NA
WP_120488296.1\|840215_841403_-	elongation factor Tu	A0A142CJQ8	Brazilian_marseillevirus	1.5e-16	26.0
WP_160224036.1\|842175_842466_-	HPF/RaiA family ribosome-associated protein	NA	NA	NA	NA
WP_160224037.1\|842490_843375_-\|integrase	tyrosine-type recombinase/integrase	A0A0K2CP59	Brevibacillus_phage	1.4e-16	24.8
WP_120488293.1\|843459_843657_-	30S ribosomal protein S21	NA	NA	NA	NA
WP_160224038.1\|843777_846930_+	UvrD-helicase domain-containing protein	E3T5J8	Cafeteria_roenbergensis_virus	4.6e-09	22.0
851908:851926	attR	NA	NA	NA	NA

Anti-CRISPR protein detection

Acr ID	Acr position	Acr size	Homology with known anti	Neighbor HTH/AcRanker	Neighbor Aca	In prophage	Protospacer in prophage

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. NZ_CP029149

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CRISPR-Cas detection and classification

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Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

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Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection